Valosin-containing protein: Difference between revisions
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'''Transitional endoplasmic reticulum ATPase''' (TER ATPase) also known as '''valosin-containing protein''' (VCP) or CDC48 in ''[[S. Cerevisiae]]'' is an [[enzyme]] that in humans is encoded by the ''VCP'' [[gene]].<ref name="pmid8595912">{{cite journal | vauthors = Druck T, Gu Y, Prabhala G, Cannizzaro LA, Park SH, Huebner K, Keen JH | title = Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP | journal = Genomics | volume = 30 | issue = 1 | pages = 94–7 | date = | '''Transitional endoplasmic reticulum ATPase''' (TER ATPase) also known as '''valosin-containing protein''' (VCP) or p97 in mammals and CDC48 in ''[[S. Cerevisiae]],'' is an [[enzyme]] that in humans is encoded by the ''VCP'' [[gene]].<ref name="pmid8595912">{{cite journal | vauthors = Druck T, Gu Y, Prabhala G, Cannizzaro LA, Park SH, Huebner K, Keen JH | title = Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP | journal = Genomics | volume = 30 | issue = 1 | pages = 94–7 | date = November 1995 | pmid = 8595912 | pmc = | doi = 10.1006/geno.1995.0016 }}</ref><ref name = "Rabouille_1995"/><ref name="entrez">{{cite web | title = Entrez Gene: VCP valosin-containing protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7415| access-date = }}</ref> The TER ATPase is an [[ATPase]] enzyme present in all [[eukaryote]]s and [[archaebacteria]]. Its main function is to segregate protein molecules from large cellular structures such as protein assemblies, organelle membranes and [[chromatin]], and thus facilitate the degradation of released polypeptides by the multi-subunit protease [[proteasome]]. | ||
p97/[[CDC48 N-terminal domain|CDC48]] is a member of the [[AAA+]] (extended family of ATPases associated with various cellular activities) ATPase family. Enzymes of this family are found in all species from bacteria to humans. Many of them are important [[chaperone (protein)|chaperones]] that regulate folding or unfolding of substrate proteins. p97/CDC48 is a type II AAA+ ATPase, which means that it contains two tandem ATPase domains (named D1 and D2, respectively) ('''Figure 1'''). [[File:VCP Wiki Figure 1.jpg|thumb|Figure 1- A schematic diagram of the p97 domain structure.]] The two ATPase domains are connected by a short polypeptide linker. A domain preceding the D1 domain ([[N-terminal]] domain) and a short [[carboxyl-terminal]] tail are involved in interaction with cofactors.<ref name = "Ogura_2001"/> The N-domain is connected to the D1 domain by a short N-D1 linker. | p97/[[CDC48 N-terminal domain|CDC48]] is a member of the [[AAA+]] (extended family of ATPases associated with various cellular activities) ATPase family. Enzymes of this family are found in all species from bacteria to humans. Many of them are important [[chaperone (protein)|chaperones]] that regulate folding or unfolding of substrate proteins. p97/CDC48 is a type II AAA+ ATPase, which means that it contains two tandem ATPase domains (named D1 and D2, respectively) ('''Figure 1'''). [[File:VCP Wiki Figure 1.jpg|thumb|Figure 1- A schematic diagram of the p97 domain structure.]] The two ATPase domains are connected by a short polypeptide linker. A domain preceding the D1 domain ([[N-terminal]] domain) and a short [[carboxyl-terminal]] tail are involved in interaction with cofactors.<ref name = "Ogura_2001"/> The N-domain is connected to the D1 domain by a short N-D1 linker. | ||
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The ATP hydrolyzing activity is indispensable for the p97/CDC48 functions.<ref name = "Wang_2004"/> The two ATPase domains of p97 (D1 and D2) are not equivalent because the D2 domain displays higher ATPase activity than the D1 domain in wild-type protein. Nevertheless, their activities are dependent of each other.<ref name = "Nishikori_2011"/><ref name = "Tang_2013"/><ref name = "Ye_2003"/><ref name = "Song_2003"/> For example, nucleotide binding to the D1 domain is required for ATP binding to the D2 domain and nucleotide binding and hydrolysis in D2 is required for the D1 domain to hydrolyze ATP. | The ATP hydrolyzing activity is indispensable for the p97/CDC48 functions.<ref name = "Wang_2004"/> The two ATPase domains of p97 (D1 and D2) are not equivalent because the D2 domain displays higher ATPase activity than the D1 domain in wild-type protein. Nevertheless, their activities are dependent of each other.<ref name = "Nishikori_2011"/><ref name = "Tang_2013"/><ref name = "Ye_2003"/><ref name = "Song_2003"/> For example, nucleotide binding to the D1 domain is required for ATP binding to the D2 domain and nucleotide binding and hydrolysis in D2 is required for the D1 domain to hydrolyze ATP. | ||
The ATPase activity of p97 can be influenced by many factors. For example, it can be stimulated by heat<ref name = "Song_2003"/> or by a putative substrate protein.<ref name = "DeLaBarre_2006b"/> | The ATPase activity of p97 can be influenced by many factors. For example, it can be stimulated by heat<ref name = "Song_2003"/> or by a putative substrate protein.<ref name = "DeLaBarre_2006b"/> In ''Leishmania infantum'', the ''Li''VCP protein is essential for the intracellular development of the parasite and its survival under heat stress.<ref name=pmid29895095>{{cite journal | vauthors = Guedes Aguiar B, Padmanabhan PK, Dumas C, Papadopoulou B | title = Valosin-containing protein VCP/p97 is essential for the intracellular development of Leishmania and its survival under heat stress | journal = Cellular Microbiology | pages = e12867 | date = June 2018 | pmid = 29895095 | doi = 10.1111/cmi.12867 }}</ref> Association with cofactors can have either positive or negative impact on the p97 ATPase activity.<ref name = "Meyer_1998"/><ref name = "Zhang_2015"/> | ||
Mutations in p97 can also influence its activity. For example, p97 mutant proteins carrying single point mutations found in patients with IBMPFD (inclusion body myopathy associated with Paget disease of the bone and frontotemporal dementia) (see below) have 2-3fold increase in ATPase activity.<ref name = "Tang_2013"/><ref name = "Halawani_2009"/><ref name = "Weihl_2006"/> | Mutations in p97 can also influence its activity. For example, p97 mutant proteins carrying single point mutations found in patients with IBMPFD (inclusion body myopathy associated with Paget disease of the bone and frontotemporal dementia) (see below) have 2-3fold increase in ATPase activity.<ref name = "Tang_2013"/><ref name = "Halawani_2009"/><ref name = "Weihl_2006"/> | ||
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=== Links to human diseases === | === Links to human diseases === | ||
Mutations in VCP cause [[multisystem proteinopathy]] (MSP), a dominantly inherited, pleiotropic, degenerative disorder of humans that can affect muscle, bone and/or the central nervous system.<ref name="Taylor2015">{{cite journal |vauthors=Taylor JP |title=Multisystem proteinopathy: | Mutations in VCP cause [[multisystem proteinopathy]] (MSP), a dominantly inherited, pleiotropic, degenerative disorder of humans that can affect muscle, bone and/or the central nervous system.<ref name="Taylor2015">{{cite journal | vauthors = Taylor JP | title = Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration | journal = Neurology | volume = 85 | issue = 8 | pages = 658–60 | date = August 2015 | pmid = 26208960 | doi = 10.1212/WNL.0000000000001862 }}</ref><ref>{{cite journal | vauthors = Kim HJ, Kim NC, Wang YD, Scarborough EA, Moore J, Diaz Z, MacLea KS, Freibaum B, Li S, Molliex A, Kanagaraj AP, Carter R, Boylan KB, Wojtas AM, Rademakers R, Pinkus JL, Greenberg SA, Trojanowski JQ, Traynor BJ, Smith BN, Topp S, Gkazi AS, Miller J, Shaw CE, Kottlors M, Kirschner J, Pestronk A, Li YR, Ford AF, Gitler AD, Benatar M, King OD, Kimonis VE, Ross ED, Weihl CC, Shorter J, Taylor JP | display-authors = 6 | title = Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS | journal = Nature | volume = 495 | issue = 7442 | pages = 467–73 | date = March 2013 | pmid = 23455423 | pmc = 3756911 | doi = 10.1038/nature11922 | bibcode = 2013Natur.495..467K }}</ref> MSP can manifest clinically as classical [[amyotrophic lateral sclerosis]] (ALS), [[frontotemporal dementia]] (FTD), [[inclusion body myopathy]] (IBM), [[Paget's disease of bone]] (PDB), or as a combination of these disorders.<ref name=pmid23635965>{{cite journal | vauthors = Benatar M, Wuu J, Fernandez C, Weihl CC, Katzen H, Steele J, Oskarsson B, Taylor JP | title = Motor neuron involvement in multisystem proteinopathy: implications for ALS | journal = Neurology | volume = 80 | issue = 20 | pages = 1874–80 | date = May 2013 | pmid = 23635965 | pmc = 3908355 | doi = 10.1212/WNL.0b013e3182929fc3 }}</ref> A useful operational definition of MSP is dominantly inherited degeneration that includes neurological involvement (either motor neuron disease or dementia) in combination with either distal myopathy or Pagetic bone degeneration.<ref name="Taylor2015" /> Most MSP patients present with weakness and of these ~65% present with motor neuron involvement.<ref name=pmid23635965/> Up to 30% of MSP patients may have exclusively motor neuron involvement.<ref name=pmid23635965/> Although MSP is rare, growing interest in this syndrome derives from the molecular insights the condition provides into the etiological relationship between common age-related degenerative diseases of muscle, bone and brain. It has been estimated that ~50% of MSP may be caused by missense mutations affecting the valosin-containing protein (VCP) gene.<ref>{{cite journal | vauthors = Le Ber I, Van Bortel I, Nicolas G, Bouya-Ahmed K, Camuzat A, Wallon D, De Septenville A, Latouche M, Lattante S, Kabashi E, Jornea L, Hannequin D, Brice A | title = hnRNPA2B1 and hnRNPA1 mutations are rare in patients with "multisystem proteinopathy" and frontotemporal lobar degeneration phenotypes | journal = Neurobiology of Aging | volume = 35 | issue = 4 | pages = 934.e5-6 | date = April 2014 | pmid = 24119545 | doi = 10.1016/j.neurobiolaging.2013.09.016 }}</ref> | ||
=== Cancer therapy === | === Cancer therapy === | ||
The first p97 inhibitor Eeyarestatin (EerI) was discovered by screening and characterizing compounds that inhibit the degradation of a fluorescence-labeled ERAD substrate.<ref name = "Fiebiger_2004"/><ref name = "Wang_2010"/> The mechanism of p97 inhibition by EerI is unclear, but when applied to cells, it induces biological phenotypes associated with p97 inhibition such as ERAD inhibition, ER stress elevation, and apoptosis induction. Importantly, EerI displays significant cancer-killing activity ''in vitro'' preferentially against cancer cells isolated from patients, and it can synergize with the proteasome inhibitor | The first p97 inhibitor [[Eeyarestatin]] (EerI) was discovered by screening and characterizing compounds that inhibit the degradation of a fluorescence-labeled ERAD substrate.<ref name = "Fiebiger_2004"/><ref name = "Wang_2010"/> The mechanism of p97 inhibition by EerI is unclear, but when applied to cells, it induces biological phenotypes associated with p97 inhibition such as ERAD inhibition, ER stress elevation, and apoptosis induction. Importantly, EerI displays significant cancer-killing activity ''in vitro'' preferentially against cancer cells isolated from patients, and it can synergize with the proteasome inhibitor [[bortezomib]] to kill cancer cells.<ref name = "Wang_2009"/> These observations prompt the idea of targeting p97 as a potential cancer therapy. This idea was further confirmed by studying several ATP competitive and allosteric inhibitors.<ref name = "Chou_2013"/><ref name = "Chou_2011"/><ref name = "Magnaghi_2013"/> More recently, a potent and specific p97 inhibitor CB-5083 has been developed, which demonstrates promising anti-cancer activities in mouse xenograft tumor models.<ref name = "Anderson_2015"/> The compound is now being evaluated in a phase 1 clinical trial.<ref name = "Nold_2016">{{cite journal | vauthors = Zhou HJ, Wang J, Yao B, Wong S, Djakovic S, Kumar B, Rice J, Valle E, Soriano F, Menon MK, Madriaga A, Kiss von Soly S, Kumar A, Parlati F, Yakes FM, Shawver L, Le Moigne R, Anderson DJ, Rolfe M, Wustrow D | title = Discovery of a First-in-Class, Potent, Selective, and Orally Bioavailable Inhibitor of the p97 AAA ATPase (CB-5083) | journal = Journal of Medicinal Chemistry | volume = 58 | issue = 24 | pages = 9480–97 | date = December 2015 | pmid = 26565666 | doi = 10.1021/acs.jmedchem.5b01346 }}</ref> | ||
==Notes== | ==Notes== | ||
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{{reflist|33em|refs= | {{reflist|33em|refs= | ||
01 <ref name = "Moir_1982">{{cite journal | vauthors = Moir D, Stewart SE, Osmond BC, Botstein D | title = Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies | journal = Genetics | volume = 100 | issue = 4 | pages = 547–63 | date = | 01 <ref name = "Moir_1982">{{cite journal | vauthors = Moir D, Stewart SE, Osmond BC, Botstein D | title = Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies | journal = Genetics | volume = 100 | issue = 4 | pages = 547–63 | date = April 1982 | pmid = 6749598 | pmc = 1201831 }}</ref> | ||
02 <ref name = "Koller_1987">{{cite journal | vauthors = Koller KJ, Brownstein MJ | title = Use of a cDNA clone to identify a supposed precursor protein containing valosin | journal = Nature | volume = 325 | issue = 6104 | pages = 542–5 | date = 1987 | pmid = 3468358 | doi = 10.1038/325542a0 | bibcode = 1987Natur.325..542K }}</ref> | 02 <ref name = "Koller_1987">{{cite journal | vauthors = Koller KJ, Brownstein MJ | title = Use of a cDNA clone to identify a supposed precursor protein containing valosin | journal = Nature | volume = 325 | issue = 6104 | pages = 542–5 | date = 1987 | pmid = 3468358 | doi = 10.1038/325542a0 | url = https://zenodo.org/record/1233057 | format = Submitted manuscript | bibcode = 1987Natur.325..542K }}</ref> | ||
03 <ref name = "Ogura_2001">{{cite journal | vauthors = Ogura T, Wilkinson AJ | title = AAA+ superfamily ATPases: common structure--diverse function | journal = Genes to Cells | volume = 6 | issue = 7 | pages = 575–97 | date = | 03 <ref name = "Ogura_2001">{{cite journal | vauthors = Ogura T, Wilkinson AJ | title = AAA+ superfamily ATPases: common structure--diverse function | journal = Genes to Cells | volume = 6 | issue = 7 | pages = 575–97 | date = July 2001 | pmid = 11473577 | doi = 10.1046/j.1365-2443.2001.00447.x }}</ref> | ||
04 <ref name = "Acharya_1995">{{cite journal | vauthors = Acharya U, Jacobs R, Peters JM, Watson N, Farquhar MG, Malhotra V | title = The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events | journal = Cell | volume = 82 | issue = 6 | pages = 895–904 | date = | 04 <ref name = "Acharya_1995">{{cite journal | vauthors = Acharya U, Jacobs R, Peters JM, Watson N, Farquhar MG, Malhotra V | title = The formation of Golgi stacks from vesiculated Golgi membranes requires two distinct fusion events | journal = Cell | volume = 82 | issue = 6 | pages = 895–904 | date = September 1995 | pmid = 7553850 | doi = 10.1016/0092-8674(95)90269-4 }}</ref> | ||
05 <ref name = "Latterich_1995">{{cite journal | vauthors = Latterich M, Fröhlich KU, Schekman R | title = Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes | journal = Cell | volume = 82 | issue = 6 | pages = 885–93 | date = | 05 <ref name = "Latterich_1995">{{cite journal | vauthors = Latterich M, Fröhlich KU, Schekman R | title = Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes | journal = Cell | volume = 82 | issue = 6 | pages = 885–93 | date = September 1995 | pmid = 7553849 | doi = 10.1016/0092-8674(95)90268-6 }}</ref> | ||
06 <ref name = "Rabouille_1995">{{cite journal | vauthors = Rabouille C, Levine TP, Peters JM, Warren G | title = An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments | journal = Cell | volume = 82 | issue = 6 | pages = 905–14 | date = | 06 <ref name = "Rabouille_1995">{{cite journal | vauthors = Rabouille C, Levine TP, Peters JM, Warren G | title = An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments | journal = Cell | volume = 82 | issue = 6 | pages = 905–14 | date = September 1995 | pmid = 7553851 | doi = 10.1016/0092-8674(95)90270-8 }}</ref> | ||
07 <ref name = "Xu_2011">{{cite journal | vauthors = Xu S, Peng G, Wang Y, Fang S, Karbowski M | title = The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover | journal = Molecular Biology of the Cell | volume = 22 | issue = 3 | pages = 291–300 | date = | 07 <ref name = "Xu_2011">{{cite journal | vauthors = Xu S, Peng G, Wang Y, Fang S, Karbowski M | title = The AAA-ATPase p97 is essential for outer mitochondrial membrane protein turnover | journal = Molecular Biology of the Cell | volume = 22 | issue = 3 | pages = 291–300 | date = February 2011 | pmid = 21118995 | pmc = 3031461 | doi = 10.1091/mbc.E10-09-0748 }}</ref> | ||
08 <ref name = "Ramanathan_2012">{{cite journal | vauthors = Ramanathan HN, Ye Y | title = The p97 ATPase associates with EEA1 to regulate the size of early endosomes | journal = Cell Research | volume = 22 | issue = 2 | pages = 346–59 | date = | 08 <ref name = "Ramanathan_2012">{{cite journal | vauthors = Ramanathan HN, Ye Y | title = The p97 ATPase associates with EEA1 to regulate the size of early endosomes | journal = Cell Research | volume = 22 | issue = 2 | pages = 346–59 | date = February 2012 | pmid = 21556036 | pmc = 3271578 | doi = 10.1038/cr.2011.80 }}</ref> | ||
09 <ref name = "Madeo_1998">{{cite journal | vauthors = Madeo F, Schlauer J, Zischka H, Mecke D, Fröhlich KU | title = Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p | journal = Molecular Biology of the Cell | volume = 9 | issue = 1 | pages = 131–41 | date = | 09 <ref name = "Madeo_1998">{{cite journal | vauthors = Madeo F, Schlauer J, Zischka H, Mecke D, Fröhlich KU | title = Tyrosine phosphorylation regulates cell cycle-dependent nuclear localization of Cdc48p | journal = Molecular Biology of the Cell | volume = 9 | issue = 1 | pages = 131–41 | date = January 1998 | pmid = 9436996 | pmc = 25228 | doi = 10.1091/mbc.9.1.131 }}</ref> | ||
10 <ref name = "Ye_2006">{{cite journal | vauthors = Ye Y | title = Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase | journal = Journal of Structural Biology | volume = 156 | issue = 1 | pages = 29–40 | date = | 10 <ref name = "Ye_2006">{{cite journal | vauthors = Ye Y | title = Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase | journal = Journal of Structural Biology | volume = 156 | issue = 1 | pages = 29–40 | date = October 2006 | pmid = 16529947 | doi = 10.1016/j.jsb.2006.01.005 | url = https://zenodo.org/record/1259185 | format = Submitted manuscript }}</ref> | ||
11 <ref name = "DeLaBarre_2003">{{cite journal | vauthors = DeLaBarre B, Brunger AT | title = Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains | journal = Nature Structural Biology | volume = 10 | issue = 10 | pages = 856–63 | date = | 11 <ref name = "DeLaBarre_2003">{{cite journal | vauthors = DeLaBarre B, Brunger AT | title = Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains | journal = Nature Structural Biology | volume = 10 | issue = 10 | pages = 856–63 | date = October 2003 | pmid = 12949490 | doi = 10.1038/nsb972 }}</ref> | ||
12 <ref name = "Davies_2008">{{cite journal | vauthors = Davies JM, Brunger AT, Weis WI | title = Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change | journal = Structure | volume = 16 | issue = 5 | pages = 715–26 | date = May 2008 | pmid = 18462676 | doi = 10.1016/j.str.2008.02.010 }}</ref> | 12 <ref name = "Davies_2008">{{cite journal | vauthors = Davies JM, Brunger AT, Weis WI | title = Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change | journal = Structure | volume = 16 | issue = 5 | pages = 715–26 | date = May 2008 | pmid = 18462676 | doi = 10.1016/j.str.2008.02.010 }}</ref> | ||
13 <ref name = "Wang_2003">{{cite journal | vauthors = Wang Q, Song C, Li CC | title = Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities | journal = Biochemical and Biophysical Research Communications | volume = 300 | issue = 2 | pages = 253–60 | date = | 13 <ref name = "Wang_2003">{{cite journal | vauthors = Wang Q, Song C, Li CC | title = Hexamerization of p97-VCP is promoted by ATP binding to the D1 domain and required for ATPase and biological activities | journal = Biochemical and Biophysical Research Communications | volume = 300 | issue = 2 | pages = 253–60 | date = January 2003 | pmid = 12504076 | doi = 10.1016/s0006-291x(02)02840-1 | url = https://zenodo.org/record/1259533 | format = Submitted manuscript }}</ref> | ||
14 <ref name = "Beuron_2006">{{cite journal | vauthors = Beuron F, Dreveny I, Yuan X, Pye VE, McKeown C, Briggs LC, Cliff MJ, Kaneko Y, Wallis R, Isaacson RL, Ladbury JE, Matthews SJ, Kondo H, Zhang X, Freemont PS | title = Conformational changes in the AAA ATPase p97-p47 adaptor complex | journal = The EMBO Journal | volume = 25 | issue = 9 | pages = 1967–76 | date = May 2006 | pmid = 16601695 | pmc = 1456939 | doi = 10.1038/sj.emboj.7601055 }}</ref> | 14 <ref name = "Beuron_2006">{{cite journal | vauthors = Beuron F, Dreveny I, Yuan X, Pye VE, McKeown C, Briggs LC, Cliff MJ, Kaneko Y, Wallis R, Isaacson RL, Ladbury JE, Matthews SJ, Kondo H, Zhang X, Freemont PS | title = Conformational changes in the AAA ATPase p97-p47 adaptor complex | journal = The EMBO Journal | volume = 25 | issue = 9 | pages = 1967–76 | date = May 2006 | pmid = 16601695 | pmc = 1456939 | doi = 10.1038/sj.emboj.7601055 }}</ref> | ||
15 <ref name = "Beuron_2003">{{cite journal | vauthors = Beuron F, Flynn TC, Ma J, Kondo H, Zhang X, Freemont PS | title = Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model | journal = Journal of Molecular Biology | volume = 327 | issue = 3 | pages = 619–29 | date = | 15 <ref name = "Beuron_2003">{{cite journal | vauthors = Beuron F, Flynn TC, Ma J, Kondo H, Zhang X, Freemont PS | title = Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model | journal = Journal of Molecular Biology | volume = 327 | issue = 3 | pages = 619–29 | date = March 2003 | pmid = 12634057 | doi = 10.1016/s0022-2836(03)00178-5 }}</ref> | ||
16 <ref name = "DeLaBarre_2006a">{{cite journal | vauthors = DeLaBarre B, Brunger AT | title = Nucleotide dependent motion and mechanism of action of p97/VCP | journal = Journal of Molecular Biology | volume = 347 | issue = 2 | pages = 437–52 | date = | 16 <ref name = "DeLaBarre_2006a">{{cite journal | vauthors = DeLaBarre B, Brunger AT | title = Nucleotide dependent motion and mechanism of action of p97/VCP | journal = Journal of Molecular Biology | volume = 347 | issue = 2 | pages = 437–52 | date = March 2005 | pmid = 15740751 | doi = 10.1016/j.jmb.2005.01.060 }}</ref> | ||
17 <ref name = "Rouiller_2002">{{cite journal | vauthors = Rouiller I, DeLaBarre B, May AP, Weis WI, Brunger AT, Milligan RA, Wilson-Kubalek EM | title = Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle | journal = Nature Structural Biology | volume = 9 | issue = 12 | pages = 950–7 | date = | 17 <ref name = "Rouiller_2002">{{cite journal | vauthors = Rouiller I, DeLaBarre B, May AP, Weis WI, Brunger AT, Milligan RA, Wilson-Kubalek EM | title = Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle | journal = Nature Structural Biology | volume = 9 | issue = 12 | pages = 950–7 | date = December 2002 | pmid = 12434150 | doi = 10.1038/nsb872 }}</ref> | ||
18 <ref name = "Tang_23010">{{cite journal | vauthors = Tang WK, Li D, Li CC, Esser L, Dai R, Guo L, Xia D | title = A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants | journal = The EMBO Journal | volume = 29 | issue = 13 | pages = 2217–29 | date = | 18 <ref name = "Tang_23010">{{cite journal | vauthors = Tang WK, Li D, Li CC, Esser L, Dai R, Guo L, Xia D | title = A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants | journal = The EMBO Journal | volume = 29 | issue = 13 | pages = 2217–29 | date = July 2010 | pmid = 20512113 | pmc = 2905243 | doi = 10.1038/emboj.2010.104 }}</ref> | ||
19 <ref name = "Wang_2004">{{cite journal | vauthors = Wang Q, Song C, Li CC | title = Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions | journal = Journal of Structural Biology | volume = 146 | issue = | 19 <ref name = "Wang_2004">{{cite journal | vauthors = Wang Q, Song C, Li CC | title = Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions | journal = Journal of Structural Biology | volume = 146 | issue = 1-2 | pages = 44–57 | year = 2004 | pmid = 15037236 | doi = 10.1016/j.jsb.2003.11.014 | url = https://zenodo.org/record/1259179 | format = Submitted manuscript }}</ref> | ||
20 <ref name = "Nishikori_2011">{{cite journal | vauthors = Nishikori S, Esaki M, Yamanaka K, Sugimoto S, Ogura T | title = Positive cooperativity of the p97 AAA ATPase is critical for essential functions | journal = The Journal of Biological Chemistry | volume = 286 | issue = 18 | pages = 15815–20 | date = May 2011 | pmid = 21454554 | pmc = 3091191 | doi = 10.1074/jbc.M110.201400 }}</ref> | 20 <ref name = "Nishikori_2011">{{cite journal | vauthors = Nishikori S, Esaki M, Yamanaka K, Sugimoto S, Ogura T | title = Positive cooperativity of the p97 AAA ATPase is critical for essential functions | journal = The Journal of Biological Chemistry | volume = 286 | issue = 18 | pages = 15815–20 | date = May 2011 | pmid = 21454554 | pmc = 3091191 | doi = 10.1074/jbc.M110.201400 }}</ref> | ||
21 <ref name = "Tang_2013">{{cite journal | vauthors = Tang WK, Xia D | title = Altered intersubunit communication is the molecular basis for functional defects of pathogenic p97 mutants | journal = The Journal of Biological Chemistry | volume = 288 | issue = 51 | pages = 36624–35 | date = | 21 <ref name = "Tang_2013">{{cite journal | vauthors = Tang WK, Xia D | title = Altered intersubunit communication is the molecular basis for functional defects of pathogenic p97 mutants | journal = The Journal of Biological Chemistry | volume = 288 | issue = 51 | pages = 36624–35 | date = December 2013 | pmid = 24196964 | pmc = 3868774 | doi = 10.1074/jbc.M113.488924 }}</ref> | ||
22 <ref name = "Ye_2003">{{cite journal | vauthors = Ye Y, Meyer HH, Rapoport TA | title = Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains | journal = The Journal of Cell Biology | volume = 162 | issue = 1 | pages = 71–84 | date = | 22 <ref name = "Ye_2003">{{cite journal | vauthors = Ye Y, Meyer HH, Rapoport TA | title = Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains | journal = The Journal of Cell Biology | volume = 162 | issue = 1 | pages = 71–84 | date = July 2003 | pmid = 12847084 | pmc = 2172719 | doi = 10.1083/jcb.200302169 }}</ref> | ||
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55 <ref name = "Chou_2013">{{cite journal | vauthors = Chou TF, Li K, Frankowski KJ, Schoenen FJ, Deshaies RJ | title = Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase | journal = ChemMedChem | volume = 8 | issue = 2 | pages = 297–312 | date = | 55 <ref name = "Chou_2013">{{cite journal | vauthors = Chou TF, Li K, Frankowski KJ, Schoenen FJ, Deshaies RJ | title = Structure-activity relationship study reveals ML240 and ML241 as potent and selective inhibitors of p97 ATPase | journal = ChemMedChem | volume = 8 | issue = 2 | pages = 297–312 | date = February 2013 | pmid = 23316025 | pmc = 3662613 | doi = 10.1002/cmdc.201200520 }}</ref> | ||
56 <ref name = "Chou_2011">{{cite journal | vauthors = Chou TF, Brown SJ, Minond D, Nordin BE, Li K, Jones AC, Chase P, Porubsky PR, Stoltz BM, Schoenen FJ, Patricelli MP, Hodder P, Rosen H, Deshaies RJ | title = Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 108 | issue = 12 | pages = 4834–9 | date = | 56 <ref name = "Chou_2011">{{cite journal | vauthors = Chou TF, Brown SJ, Minond D, Nordin BE, Li K, Jones AC, Chase P, Porubsky PR, Stoltz BM, Schoenen FJ, Patricelli MP, Hodder P, Rosen H, Deshaies RJ | title = Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 108 | issue = 12 | pages = 4834–9 | date = March 2011 | pmid = 21383145 | pmc = 3064330 | doi = 10.1073/pnas.1015312108 | bibcode = 2011PNAS..108.4834C }}</ref> | ||
57 <ref name = "Magnaghi_2013">{{cite journal | vauthors = Magnaghi P, D'Alessio R, Valsasina B, Avanzi N, Rizzi S, Asa D, Gasparri F, Cozzi L, Cucchi U, Orrenius C, Polucci P, Ballinari D, Perrera C, Leone A, Cervi G, Casale E, Xiao Y, Wong C, Anderson DJ, Galvani A, Donati D, O'Brien T, Jackson PK, Isacchi A | title = Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death | journal = Nature Chemical Biology | volume = 9 | issue = 9 | pages = 548–56 | date = | 57 <ref name = "Magnaghi_2013">{{cite journal | vauthors = Magnaghi P, D'Alessio R, Valsasina B, Avanzi N, Rizzi S, Asa D, Gasparri F, Cozzi L, Cucchi U, Orrenius C, Polucci P, Ballinari D, Perrera C, Leone A, Cervi G, Casale E, Xiao Y, Wong C, Anderson DJ, Galvani A, Donati D, O'Brien T, Jackson PK, Isacchi A | title = Covalent and allosteric inhibitors of the ATPase VCP/p97 induce cancer cell death | journal = Nature Chemical Biology | volume = 9 | issue = 9 | pages = 548–56 | date = September 2013 | pmid = 23892893 | doi = 10.1038/nchembio.1313 }}</ref> | ||
58 <ref name = "Anderson_2015">{{cite journal | vauthors = Anderson DJ, Le Moigne R, Djakovic S, Kumar B, Rice J, Wong S, Wang J, Yao B, Valle E, Kiss von Soly S, Madriaga A, Soriano F, Menon MK, Wu ZY, Kampmann M, Chen Y, Weissman JS, Aftab BT, Yakes FM, Shawver L, Zhou HJ, Wustrow D, Rolfe M | title = Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis | journal = Cancer Cell | volume = 28 | issue = 5 | pages = | 58 <ref name = "Anderson_2015">{{cite journal | vauthors = Anderson DJ, Le Moigne R, Djakovic S, Kumar B, Rice J, Wong S, Wang J, Yao B, Valle E, Kiss von Soly S, Madriaga A, Soriano F, Menon MK, Wu ZY, Kampmann M, Chen Y, Weissman JS, Aftab BT, Yakes FM, Shawver L, Zhou HJ, Wustrow D, Rolfe M | title = Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis | journal = Cancer Cell | volume = 28 | issue = 5 | pages = 653–665 | date = November 2015 | pmid = 26555175 | pmc = 4941640 | doi = 10.1016/j.ccell.2015.10.002 }}</ref> | ||
}} | }} | ||
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== Further reading == | == Further reading == | ||
{{refbegin|33em}} | {{refbegin|33em}} | ||
* {{cite journal | vauthors = Guinto JB, Ritson GP, Taylor JP, Forman MS | title = Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy | journal = Acta Neuropathologica | volume = 114 | issue = 1 | pages = 55–61 | date = | * {{cite journal | vauthors = Guinto JB, Ritson GP, Taylor JP, Forman MS | title = Valosin-containing protein and the pathogenesis of frontotemporal dementia associated with inclusion body myopathy | journal = Acta Neuropathologica | volume = 114 | issue = 1 | pages = 55–61 | date = July 2007 | pmid = 17457594 | doi = 10.1007/s00401-007-0224-7 }} | ||
* {{cite journal | vauthors = Dawson SJ, White LA | title = Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin | journal = The Journal of Infection | volume = 24 | issue = 3 | pages = 317–20 | date = May 1992 | pmid = 1602151 | doi = 10.1016/S0163-4453(05)80037-4 }} | * {{cite journal | vauthors = Dawson SJ, White LA | title = Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin | journal = The Journal of Infection | volume = 24 | issue = 3 | pages = 317–20 | date = May 1992 | pmid = 1602151 | doi = 10.1016/S0163-4453(05)80037-4 }} | ||
* {{cite journal | vauthors = Pleasure IT, Black MM, Keen JH | title = Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein | journal = Nature | volume = 365 | issue = 6445 | pages = 459–62 | date = | * {{cite journal | vauthors = Pleasure IT, Black MM, Keen JH | title = Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein | journal = Nature | volume = 365 | issue = 6445 | pages = 459–62 | date = September 1993 | pmid = 8413590 | doi = 10.1038/365459a0 | bibcode = 1993Natur.365..459P }} | ||
* {{cite journal | vauthors = Germain-Lee EL, Obie C, Valle D | title = NVL: a new member of the AAA family of ATPases localized to the nucleus | journal = Genomics | volume = 44 | issue = 1 | pages = 22–34 | date = | * {{cite journal | vauthors = Germain-Lee EL, Obie C, Valle D | title = NVL: a new member of the AAA family of ATPases localized to the nucleus | journal = Genomics | volume = 44 | issue = 1 | pages = 22–34 | date = August 1997 | pmid = 9286697 | doi = 10.1006/geno.1997.4856 }} | ||
* {{cite journal | vauthors = Hoyle J, Tan KH, Fisher EM | title = Mapping the valosin-containing protein (VCP) gene on human chromosome 9 and mouse chromosome 4, and a likely pseudogene on the mouse X chromosome | journal = Mammalian Genome | volume = 8 | issue = 10 | pages = 778–80 | date = | * {{cite journal | vauthors = Hoyle J, Tan KH, Fisher EM | title = Mapping the valosin-containing protein (VCP) gene on human chromosome 9 and mouse chromosome 4, and a likely pseudogene on the mouse X chromosome | journal = Mammalian Genome | volume = 8 | issue = 10 | pages = 778–80 | date = October 1997 | pmid = 9321476 | doi = 10.1007/s003359900566 }} | ||
* {{cite journal | vauthors = Dai RM, Chen E, Longo DL, Gorbea CM, Li CC | title = Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha | journal = The Journal of Biological Chemistry | volume = 273 | issue = 6 | pages = 3562–73 | date = | * {{cite journal | vauthors = Dai RM, Chen E, Longo DL, Gorbea CM, Li CC | title = Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha | journal = The Journal of Biological Chemistry | volume = 273 | issue = 6 | pages = 3562–73 | date = February 1998 | pmid = 9452483 | doi = 10.1074/jbc.273.6.3562 }} | ||
* {{cite journal | vauthors = Rabouille C, Kondo H, Newman R, Hui N, Freemont P, Warren G | title = Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro | journal = Cell | volume = 92 | issue = 5 | pages = 603–10 | date = | * {{cite journal | vauthors = Rabouille C, Kondo H, Newman R, Hui N, Freemont P, Warren G | title = Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly pathways of Golgi cisternae from mitotic Golgi fragments in vitro | journal = Cell | volume = 92 | issue = 5 | pages = 603–10 | date = March 1998 | pmid = 9506515 | doi = 10.1016/S0092-8674(00)81128-9 }} | ||
* {{cite journal | vauthors = Zhang SH, Liu J, Kobayashi R, Tonks NK | title = Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 25 | pages = 17806–12 | date = | * {{cite journal | vauthors = Zhang SH, Liu J, Kobayashi R, Tonks NK | title = Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 25 | pages = 17806–12 | date = June 1999 | pmid = 10364224 | doi = 10.1074/jbc.274.25.17806 }} | ||
* {{cite journal | vauthors = Zhang H, Wang Q, Kajino K, Greene MI | title = VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells | journal = DNA and Cell Biology | volume = 19 | issue = 5 | pages = 253–63 | date = May 2000 | pmid = 10855792 | doi = 10.1089/10445490050021168 }} | * {{cite journal | vauthors = Zhang H, Wang Q, Kajino K, Greene MI | title = VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells | journal = DNA and Cell Biology | volume = 19 | issue = 5 | pages = 253–63 | date = May 2000 | pmid = 10855792 | doi = 10.1089/10445490050021168 }} | ||
* {{cite journal | vauthors = Lavoie C, Chevet E, Roy L, Tonks NK, Fazel A, Posner BI, Paiement J, Bergeron JJ | title = Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 25 | pages = 13637–42 | date = | * {{cite journal | vauthors = Lavoie C, Chevet E, Roy L, Tonks NK, Fazel A, Posner BI, Paiement J, Bergeron JJ | title = Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 25 | pages = 13637–42 | date = December 2000 | pmid = 11087817 | pmc = 17628 | doi = 10.1073/pnas.240278097 | bibcode = 2000PNAS...9713637L }} | ||
* {{cite journal | vauthors = Seigneurin-Berny D, Verdel A, Curtet S, Lemercier C, Garin J, Rousseaux S, Khochbin S | title = Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways | journal = Molecular and Cellular Biology | volume = 21 | issue = 23 | pages = 8035–44 | date = | * {{cite journal | vauthors = Seigneurin-Berny D, Verdel A, Curtet S, Lemercier C, Garin J, Rousseaux S, Khochbin S | title = Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways | journal = Molecular and Cellular Biology | volume = 21 | issue = 23 | pages = 8035–44 | date = December 2001 | pmid = 11689694 | pmc = 99970 | doi = 10.1128/MCB.21.23.8035-8044.2001 }} | ||
* {{cite journal | vauthors = Yang CS, Weiner H | title = Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol | journal = Archives of Biochemistry and Biophysics | volume = 400 | issue = 1 | pages = 105–10 | date = | * {{cite journal | vauthors = Yang CS, Weiner H | title = Yeast two-hybrid screening identifies binding partners of human Tom34 that have ATPase activity and form a complex with Tom34 in the cytosol | journal = Archives of Biochemistry and Biophysics | volume = 400 | issue = 1 | pages = 105–10 | date = April 2002 | pmid = 11913976 | doi = 10.1006/abbi.2002.2778 }} | ||
* {{cite journal | vauthors = Asai T, Tomita Y, Nakatsuka S, Hoshida Y, Myoui A, Yoshikawa H, Aozasa K | title = VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line | journal = Japanese Journal of Cancer Research | volume = 93 | issue = 3 | pages = 296–304 | date = | * {{cite journal | vauthors = Asai T, Tomita Y, Nakatsuka S, Hoshida Y, Myoui A, Yoshikawa H, Aozasa K | title = VCP (p97) regulates NFkappaB signaling pathway, which is important for metastasis of osteosarcoma cell line | journal = Japanese Journal of Cancer Research | volume = 93 | issue = 3 | pages = 296–304 | date = March 2002 | pmid = 11927012 | pmc = 5926968 | doi = 10.1111/j.1349-7006.2002.tb02172.x }} | ||
* {{cite journal | vauthors = Kobayashi T, Tanaka K, Inoue K, Kakizuka A | title = Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells | journal = The Journal of Biological Chemistry | volume = 277 | issue = 49 | pages = 47358–65 | date = | * {{cite journal | vauthors = Kobayashi T, Tanaka K, Inoue K, Kakizuka A | title = Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells | journal = The Journal of Biological Chemistry | volume = 277 | issue = 49 | pages = 47358–65 | date = December 2002 | pmid = 12351637 | doi = 10.1074/jbc.M207783200 }} | ||
* {{cite journal | vauthors = Uchiyama K, Jokitalo E, Kano F, Murata M, Zhang X, Canas B, Newman R, Rabouille C, Pappin D, Freemont P, Kondo H | title = VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo | journal = The Journal of Cell Biology | volume = 159 | issue = 5 | pages = 855–66 | date = | * {{cite journal | vauthors = Uchiyama K, Jokitalo E, Kano F, Murata M, Zhang X, Canas B, Newman R, Rabouille C, Pappin D, Freemont P, Kondo H | title = VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo | journal = The Journal of Cell Biology | volume = 159 | issue = 5 | pages = 855–66 | date = December 2002 | pmid = 12473691 | pmc = 2173386 | doi = 10.1083/jcb.200208112 }} | ||
{{refend}} | {{refend}} | ||
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Transitional endoplasmic reticulum ATPase (TER ATPase) also known as valosin-containing protein (VCP) or p97 in mammals and CDC48 in S. Cerevisiae, is an enzyme that in humans is encoded by the VCP gene.[1][2][3] The TER ATPase is an ATPase enzyme present in all eukaryotes and archaebacteria. Its main function is to segregate protein molecules from large cellular structures such as protein assemblies, organelle membranes and chromatin, and thus facilitate the degradation of released polypeptides by the multi-subunit protease proteasome.
p97/CDC48 is a member of the AAA+ (extended family of ATPases associated with various cellular activities) ATPase family. Enzymes of this family are found in all species from bacteria to humans. Many of them are important chaperones that regulate folding or unfolding of substrate proteins. p97/CDC48 is a type II AAA+ ATPase, which means that it contains two tandem ATPase domains (named D1 and D2, respectively) (Figure 1).
The two ATPase domains are connected by a short polypeptide linker. A domain preceding the D1 domain (N-terminal domain) and a short carboxyl-terminal tail are involved in interaction with cofactors.[4] The N-domain is connected to the D1 domain by a short N-D1 linker.
Most known substrates of p97/CDC48 are modified with ubiquitin chains and degraded by the 26S proteasome. Accordingly, many p97/CDC48 coenzymes and adaptors have domains that can recognize ubiquitin.[5] It has become evident that the interplays between ubiquitin and p97/CDC48 cofactors are critical for many of the proposed functions, although the precise role of these interactions remains to be elucidated.
Discovery
CDC48 was discovered in a genetic screen for genes involved in cell cycle regulation in budding yeast.[6] The screen identified several alleles of Cdc48 that affects cell growth at non-permissive temperatures. The mammalian homolog of CDC48 was initially characterized as a 97 kDa protein precursor for the small peptide valosin. It was therefore named as valosin-containing protein (VCP) or p97,[7] but subsequent studies showed that valosin is an artifact of purification unrelated to p97. Nevertheless, the VCP nomenclature is still being used in the literature.
Tissue and subcelluar distribution
p97/CDC48 is one of the most abundant cytoplasmic proteins in eukaryotic cells. It is ubiquitously expressed in all tissues in multicellular organisms. In humans, the mRNA expression of p97 was found to be moderately elevated in certain types of cancer.[5]
In mammalian cells, p97 is predominantly localized to the cytoplasm, and a significant fraction is associated to membranes of cellular organelles such as the endoplasmic reticulum (ER), Golgi, mitochondria, and endosomes.[2][8][9][10][11] The subcellular localization of CDC48 has not been fully characterized, but is likely to be similar to the mammalian counterpart. A fraction of p97/CDC48 was also found in the nucleus.[12]
Structure
According to the crystal structures of full-length wild-type p97,[13][14] six p97 subunits assemble into a barrel-like structure, in which the N-D1 and D2 domains form two concentric, stacked rings (Figure 2).
The N-D1 ring is larger (162 Å in diameter) than the D2 ring (113 Å) due to the laterally attached N-domains. The D1 and D2 domains are highly homologous in both sequence and structure, but they serve distinct functions. For example, the hexameric assembly of p97 only requires the D1 but not the D2 domain.[15] Unlike many bacterial AAA+ proteins, assembly of p97 hexamer does not depend on the presence of nucleotide. The p97 hexameric assembly can undergo dramatic conformational changes during nucleotide hydrolysis cycle,[16][17][18][19][20] and it is generally believed that these conformational changes generate mechanical force, which is applied to substrate molecules to influence their stability and function. However, how precisely p97 generates force is unclear.
The ATP hydrolysis cycle
The ATP hydrolyzing activity is indispensable for the p97/CDC48 functions.[21] The two ATPase domains of p97 (D1 and D2) are not equivalent because the D2 domain displays higher ATPase activity than the D1 domain in wild-type protein. Nevertheless, their activities are dependent of each other.[22][23][24][25] For example, nucleotide binding to the D1 domain is required for ATP binding to the D2 domain and nucleotide binding and hydrolysis in D2 is required for the D1 domain to hydrolyze ATP.
The ATPase activity of p97 can be influenced by many factors. For example, it can be stimulated by heat[25] or by a putative substrate protein.[26] In Leishmania infantum, the LiVCP protein is essential for the intracellular development of the parasite and its survival under heat stress.[27] Association with cofactors can have either positive or negative impact on the p97 ATPase activity.[28][29]
Mutations in p97 can also influence its activity. For example, p97 mutant proteins carrying single point mutations found in patients with IBMPFD (inclusion body myopathy associated with Paget disease of the bone and frontotemporal dementia) (see below) have 2-3fold increase in ATPase activity.[23][30][31]
p97/CDC48-interacting proteins
Recent proteomic studies have identified a large number of p97-interacting proteins. Many of these proteins serve as adaptors that link p97/CDC48 to a particular subcellular compartment to function in a specific cellular pathway. Others function as adaptors that recruit substrates to p97/CDC48 for processing. Some p97-interacting proteins are also enzymes such as N-glycanase, ubiquitin ligase, and deubiquitinase, which assist p97 in processing substrates.
Most cofactors bind p97/CDC48 through its N-domain, but a few interact with the short carboxy-terminal tail in p97/CDC48. Representative proteins interacting with the N-domain are Ufd1, Npl4, p47 and FAF1.[32][33][34] Examples of cofactors that interact with the carboxy-terminal tail of p97 are PLAA, PNGase, and Ufd2.[35][36][37]
The molecular basis for cofactor binding has been studied for some cofactors that interact with the p97 N-domain. The N-domain consists of two sub-domains of roughly equal size: the N-terminal double Y-barrel and a C-terminal b-barrel (Figure 3).
Structural studies show that many cofactor proteins bind to the N-domain at a cleft formed between the two sub-domains.
Among those that bind to the N-domain of p97, two most frequently occurring sequence motifs are found: one is called UBX motif (ubiquitin regulatory X)[38] and the other is termed VIM (VCP-interacting motif).[39] The UBX domain is an 80-residue module with a fold highly resembling the structure of ubiquitin. The VCP-interacting motif (VIM) is a linear sequence motif (RX5AAX2R) found in a number of p97 cofactors including gp78,[40] SVIP (small VCP-inhibiting protein)[41] and VIMP (VCP interacting membrane protein).[42] Although the UBX domain uses a surface loop whereas the VIM forms a-helix to bind p97, both UBX and VIM bind at the same location between the two sub-domains of the N-domain (Figure 3).[43] It was proposed that hierarchical binding to distinct cofactors may be essential for the broad functions of p97/CDC48.[44][45]
Function
p97/CDC48 performs diverse functions through modulating the stability and thus the activity of its substrates. The general function of p97/CDC48 is to segregate proteins from large protein assembly or immobile cellular structures such as membranes or chromatin, allowing the released protein molecules to be degraded by the proteasome. The functions of p97/CDC48 can be grouped into the following three major categories.
Protein quality control
The best characterized function of p97 is to mediate a network of protein quality control processes in order to maintain protein homeostasis.[46] These include endoplasmic reticulum-associated protein degradation (ERAD) and mitochondria-associated degradation.[10][47] In these processes, ATP hydrolysis by p97/CDC48 is required to extract aberrant proteins from the membranes of the ER or mitochondria. p97/CDC48 is also required to release defective translation products stalled on ribosome in a process termed ribosome-associated degradation.[48][49][50] It appears that only after extraction from the membranes or large protein assembly like ribosome, can polypeptides be degraded by the proteasome. In addition to this ‘segregase’ function, p97/CDC48 might have an additional role in shuttling the released polypeptides to the proteasome. This chaperoning function seems to be particularly important for degradation of certain aggregation-prone misfolded proteins in nucleus.[51] Several lines of evidence also implicate p97 in autophagy, a process that turns over cellular proteins (including misfolded ones) by engulfing them into double-membrane-surrounded vesicles named autophagosome, but the precise role of p97 in this process is unclear.[52]
Chromatin-associated functions
p97 also functions broadly in eukaryotic nucleus by releasing protein molecules from chromatins in a manner analogous to that in ERAD.[53] The identified p97 substrates include transcriptional repressor α2 and RNA polymerase (Pol) II complex and CMG DNA helicase in budding yeast, and the DNA replicating licensing factor CDT1, DNA repairing proteins DDB2 and XPC, mitosis regulator Aurora B, and certain DNA polymerases in mammalian cells. These substrates link p97 function to gene transcription, DNA replication and repair, and cell cycle progression.
Membrane fusion and trafficking
Biochemical and genetic studies have also implicated p97 in fusion of vesicles that lead to the formation of Golgi apparatus at the end of mitosis.[54] This process requires the ubiquitin binding adaptor p47 and a p97-associated deubiquitinase VCIP135, and thus connecting membrane fusion to the ubiquitin pathways. However, the precise role of p97 in Golgi formation is unclear due to lack of information on relevant substrate(s). Recent studies also suggest that p97 may regulate vesicle trafficking from plasma membrane to the lysosome, a process termed endocytosis.[52]
Clinical significance
Links to human diseases
Mutations in VCP cause multisystem proteinopathy (MSP), a dominantly inherited, pleiotropic, degenerative disorder of humans that can affect muscle, bone and/or the central nervous system.[55][56] MSP can manifest clinically as classical amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), inclusion body myopathy (IBM), Paget's disease of bone (PDB), or as a combination of these disorders.[57] A useful operational definition of MSP is dominantly inherited degeneration that includes neurological involvement (either motor neuron disease or dementia) in combination with either distal myopathy or Pagetic bone degeneration.[55] Most MSP patients present with weakness and of these ~65% present with motor neuron involvement.[57] Up to 30% of MSP patients may have exclusively motor neuron involvement.[57] Although MSP is rare, growing interest in this syndrome derives from the molecular insights the condition provides into the etiological relationship between common age-related degenerative diseases of muscle, bone and brain. It has been estimated that ~50% of MSP may be caused by missense mutations affecting the valosin-containing protein (VCP) gene.[58]
Cancer therapy
The first p97 inhibitor Eeyarestatin (EerI) was discovered by screening and characterizing compounds that inhibit the degradation of a fluorescence-labeled ERAD substrate.[59][60] The mechanism of p97 inhibition by EerI is unclear, but when applied to cells, it induces biological phenotypes associated with p97 inhibition such as ERAD inhibition, ER stress elevation, and apoptosis induction. Importantly, EerI displays significant cancer-killing activity in vitro preferentially against cancer cells isolated from patients, and it can synergize with the proteasome inhibitor bortezomib to kill cancer cells.[61] These observations prompt the idea of targeting p97 as a potential cancer therapy. This idea was further confirmed by studying several ATP competitive and allosteric inhibitors.[62][63][64] More recently, a potent and specific p97 inhibitor CB-5083 has been developed, which demonstrates promising anti-cancer activities in mouse xenograft tumor models.[65] The compound is now being evaluated in a phase 1 clinical trial.[66]
Notes
The 2015 version of this article was updated by an external expert under a dual publication model. The corresponding academic peer reviewed article was published in Gene and can be cited as: {{#property:P2093|from=Q36767612}} ({{#property:P577|from=Q36767612}}). "{{#property:P1476|from=Q36767612}}". Gene. {{#property:P478|from=Q36767612}} ({{#property:P433|from=Q36767612}}): {{#property:P304|from=Q36767612}}. doi:{{#property:P356|from=Q36767612}} Check |doi= value (help). PMC {{#property:P932|from=Q36767612}} Check |pmc= value (help). PMID {{#property:P698|from=Q36767612}} Check |pmid= value (help). Check date values in: |date= (help) |
References
- ↑ Druck T, Gu Y, Prabhala G, Cannizzaro LA, Park SH, Huebner K, Keen JH (November 1995). "Chromosome localization of human genes for clathrin adaptor polypeptides AP2 beta and AP50 and the clathrin-binding protein, VCP". Genomics. 30 (1): 94–7. doi:10.1006/geno.1995.0016. PMID 8595912.
- ↑ 2.0 2.1 Rabouille C, Levine TP, Peters JM, Warren G (September 1995). "An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments". Cell. 82 (6): 905–14. doi:10.1016/0092-8674(95)90270-8. PMID 7553851.
- ↑ "Entrez Gene: VCP valosin-containing protein".
- ↑ Ogura T, Wilkinson AJ (July 2001). "AAA+ superfamily ATPases: common structure--diverse function". Genes to Cells. 6 (7): 575–97. doi:10.1046/j.1365-2443.2001.00447.x. PMID 11473577.
- ↑ 5.0 5.1 Ye Y (October 2006). "Diverse functions with a common regulator: ubiquitin takes command of an AAA ATPase" (Submitted manuscript). Journal of Structural Biology. 156 (1): 29–40. doi:10.1016/j.jsb.2006.01.005. PMID 16529947.
- ↑ Moir D, Stewart SE, Osmond BC, Botstein D (April 1982). "Cold-sensitive cell-division-cycle mutants of yeast: isolation, properties, and pseudoreversion studies". Genetics. 100 (4): 547–63. PMC 1201831. PMID 6749598.
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Further reading
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- Dawson SJ, White LA (May 1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". The Journal of Infection. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
- Pleasure IT, Black MM, Keen JH (September 1993). "Valosin-containing protein, VCP, is a ubiquitous clathrin-binding protein". Nature. 365 (6445): 459–62. Bibcode:1993Natur.365..459P. doi:10.1038/365459a0. PMID 8413590.
- Germain-Lee EL, Obie C, Valle D (August 1997). "NVL: a new member of the AAA family of ATPases localized to the nucleus". Genomics. 44 (1): 22–34. doi:10.1006/geno.1997.4856. PMID 9286697.
- Hoyle J, Tan KH, Fisher EM (October 1997). "Mapping the valosin-containing protein (VCP) gene on human chromosome 9 and mouse chromosome 4, and a likely pseudogene on the mouse X chromosome". Mammalian Genome. 8 (10): 778–80. doi:10.1007/s003359900566. PMID 9321476.
- Dai RM, Chen E, Longo DL, Gorbea CM, Li CC (February 1998). "Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha". The Journal of Biological Chemistry. 273 (6): 3562–73. doi:10.1074/jbc.273.6.3562. PMID 9452483.
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- Zhang SH, Liu J, Kobayashi R, Tonks NK (June 1999). "Identification of the cell cycle regulator VCP (p97/CDC48) as a substrate of the band 4.1-related protein-tyrosine phosphatase PTPH1". The Journal of Biological Chemistry. 274 (25): 17806–12. doi:10.1074/jbc.274.25.17806. PMID 10364224.
- Zhang H, Wang Q, Kajino K, Greene MI (May 2000). "VCP, a weak ATPase involved in multiple cellular events, interacts physically with BRCA1 in the nucleus of living cells". DNA and Cell Biology. 19 (5): 253–63. doi:10.1089/10445490050021168. PMID 10855792.
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- Seigneurin-Berny D, Verdel A, Curtet S, Lemercier C, Garin J, Rousseaux S, Khochbin S (December 2001). "Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways". Molecular and Cellular Biology. 21 (23): 8035–44. doi:10.1128/MCB.21.23.8035-8044.2001. PMC 99970. PMID 11689694.
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- Uchiyama K, Jokitalo E, Kano F, Murata M, Zhang X, Canas B, Newman R, Rabouille C, Pappin D, Freemont P, Kondo H (December 2002). "VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo". The Journal of Cell Biology. 159 (5): 855–66. doi:10.1083/jcb.200208112. PMC 2173386. PMID 12473691.
