Profilin 1: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Profilin-1''' is a [[protein]] that in humans is encoded by the ''PFN1'' [[gene]].<ref name="pmid3356709">{{cite journal | vauthors = Kwiatkowski DJ, Bruns GA | title = Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis | journal = J Biol Chem | volume = 263 | issue = 12 | pages = 5910–5 | date = May 1988 | pmid = 3356709 | pmc =  | doi =  }}</ref><ref name="pmid1968707">{{cite journal | vauthors = Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC | title = Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome | journal = Am J Hum Genet | volume = 46 | issue = 3 | pages = 559–67 | date = April 1990 | pmid = 1968707 | pmc = 1683621 | doi = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PFN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1awi.
| PDB = {{PDB2|1awi}}, {{PDB2|1cf0}}, {{PDB2|1cjf}}, {{PDB2|1fik}}, {{PDB2|1fil}}, {{PDB2|1hlu}}, {{PDB2|1pfl}}, {{PDB2|1pne}}, {{PDB2|2btf}}
| Name = Profilin 1
| HGNCid = 8881
| Symbol = PFN1
| AltSymbols =;
| OMIM = 176610
| ECnumber = 
| Homologene = 3684
| MGIid = 97549
| GeneAtlas_image1 = PBB_GE_PFN1_200634_at_tn.png
| Function = {{GNF_GO|id=GO:0003785 |text = actin monomer binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0001843 |text = neural tube closure}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5216
    | Hs_Ensembl = ENSG00000108518
    | Hs_RefseqProtein = NP_005013
    | Hs_RefseqmRNA = NM_005022
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 4789692
    | Hs_GenLoc_end = 4793067
    | Hs_Uniprot = P07737
    | Mm_EntrezGene = 18643
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_011072
    | Mm_RefseqProtein = NP_035202
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =
  }}
}}
'''Profilin 1''', also known as '''PFN1''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. Deletion of this gene is associated with [[Miller–Dieker syndrome|Miller-Dieker syndrome]].<ref name="entrez">{{cite web | title = Entrez Gene: PFN1 profilin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5216| accessdate = }}</ref> Mutations in this gene may be a rare cause of [[amyotrophic lateral sclerosis]], also called Lou Gehrig's disease.<ref>{{cite journal | vauthors = Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, Lowe P, Koppers M, McKenna-Yasek D, Baron DM, Kost JE, Gonzalez-Perez P, Fox AD, Adams J, Taroni F, Tiloca C, Leclerc AL, Chafe SC, Mangroo D, Moore MJ, Zitzewitz JA, Xu ZS, van den Berg LH, Glass JD, Siciliano G, Cirulli ET, Goldstein DB, Salachas F, Meininger V, Rossoll W, Ratti A, Gellera C, Bosco DA, Bassell GJ, Silani V, Drory VE, Brown RH, Landers JE | display-authors = 6 | title = Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis | journal = Nature | volume = 488 | issue = 7412 | pages = 499-503 | date = August 2012 | pmid = 22801503 | pmc = 3575525 | doi = 10.1038/nature11280 }}</ref><ref>{{cite journal | vauthors = Daoud H, Dobrzeniecka S, Camu W, Meininger V, Dupré N, Dion PA, Rouleau GA | title = Mutation analysis of PFN1 in familial amyotrophic lateral sclerosis patients | journal = Neurobiology of Aging | volume = 34 | issue = 4 | pages = 1311.e1-2 | date = April 2013 | pmid = 23062600 | doi = 10.1016/j.neurobiolaging.2012.09.001 }}</ref><ref>{{cite journal | vauthors = Tiloca C, Ticozzi N, Pensato V, Corrado L, Del Bo R, Bertolin C, Fenoglio C, Gagliardi S, Calini D, Lauria G, Castellotti B, Bagarotti A, Corti S, Galimberti D, Cagnin A, Gabelli C, Ranieri M, Ceroni M, Siciliano G, Mazzini L, Cereda C, Scarpini E, Sorarù G, Comi GP, D'Alfonso S, Gellera C, Ratti A, Landers JE, Silani V | display-authors = 6 | title = Screening of the PFN1 gene in sporadic amyotrophic lateral sclerosis and in frontotemporal dementia | journal = Neurobiology of Aging | volume = 34 | issue = 5 | pages = 1517.e9-10 | date = May 2013 | pmid = 23063648 | pmc = 3548975 | doi = 10.1016/j.neurobiolaging.2012.09.016 }}</ref><ref>{{cite journal | vauthors = Ingre C, Landers JE, Rizik N, Volk AE, Akimoto C, Birve A, Hübers A, Keagle PJ, Piotrowska K, Press R, Andersen PM, Ludolph AC, Weishaupt JH | display-authors = 6 | title = A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts | journal = Neurobiology of Aging | volume = 34 | issue = 6 | pages = 1708.e1-6 | date = June 2013 | pmid = 23141414 | doi = 10.1016/j.neurobiolaging.2012.10.009 }}</ref><ref>{{cite journal | vauthors = Lattante S, Le Ber I, Camuzat A, Brice A, Kabashi E | title = Mutations in the PFN1 gene are not a common cause in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration in France | journal = Neurobiology of Aging | volume = 34 | issue = 6 | pages = 1709.e1-2 | date = June 2013 | pmid = 23182804 | doi = 10.1016/j.neurobiolaging.2012.10.026 }}</ref><ref>{{cite journal | vauthors = Dillen L, Van Langenhove T, Engelborghs S, Vandenbulcke M, Sarafov S, Tournev I, Merlin C, Cras P, Vandenberghe R, De Deyn PP, Jordanova A, Cruts M, Van Broeckhoven C, van der Zee J | display-authors = 6 | title = Explorative genetic study of UBQLN2 and PFN1 in an extended Flanders-Belgian cohort of frontotemporal lobar degeneration patients | journal = Neurobiology of Aging | volume = 34 | issue = 6 | pages = 1711.e1-5 | date = June 2013 | pmid = 23312802 | doi = 10.1016/j.neurobiolaging.2012.12.007 }}</ref><ref>{{cite journal | vauthors = Zou ZY, Sun Q, Liu MS, Li XG, Cui LY | title = Mutations in the profilin 1 gene are not common in amyotrophic lateral sclerosis of Chinese origin | journal = Neurobiology of Aging | volume = 34 | issue = 6 | pages = 1713.e5-6 | date = June 2013 | pmid = 23357624 | doi = 10.1016/j.neurobiolaging.2012.12.024 }}</ref><ref>{{cite journal | vauthors = Chen Y, Zheng ZZ, Huang R, Chen K, Song W, Zhao B, Chen X, Yang Y, Yuan L, Shang HF | display-authors = 6 | title = PFN1 mutations are rare in Han Chinese populations with amyotrophic lateral sclerosis | journal = Neurobiology of Aging | volume = 34 | issue = 7 | pages = 1922.e1-5 | date = July 2013 | pmid = 23428184 | doi = 10.1016/j.neurobiolaging.2013.01.013 }}</ref><ref>{{cite journal | vauthors = van Blitterswijk M, Baker MC, Bieniek KF, Knopman DS, Josephs KA, Boeve B, Caselli R, Wszolek ZK, Petersen R, Graff-Radford NR, Boylan KB, Dickson DW, Rademakers R | display-authors = 6 | title = Profilin-1 mutations are rare in patients with amyotrophic lateral sclerosis and frontotemporal dementia | journal = Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration | volume = 14 | issue = 5-6 | pages = 463-9 | date = September 2013 | pmid = 23634771 | pmc = 3923463 | doi = 10.3109/21678421.2013.787630 }}</ref><ref>{{cite journal | vauthors = Yang S, Fifita JA, Williams KL, Warraich ST, Pamphlett R, Nicholson GA, Blair IP | display-authors = 6 | title = Mutation analysis and immunopathological studies of PFN1 in familial and sporadic amyotrophic lateral sclerosis | journal = Neurobiology of Aging | volume = 34 | issue = 9 | pages = 2235.e7-10 | date = September 2013 | pmid = 23635659 | doi = 10.1016/j.neurobiolaging.2013.04.003 }}</ref><ref>{{cite journal | vauthors = Fratta P, Charnock J, Collins T, Devoy A, Howard R, Malaspina A, Orrell R, Sidle K, Clarke J, Shoai M, Lu CH, Hardy J, Plagnol V, Fisher EM | display-authors = 6 | title = Profilin1 E117G is a moderate risk factor for amyotrophic lateral sclerosis | journal = Journal of Neurology, Neurosurgery, and Psychiatry | volume = 85 | issue = 5 | pages = 506-8 | date = May 2014 | pmid = 24309268 | pmc = 3995330 | doi = 10.1136/jnnp-2013-306761 }}</ref><ref>{{cite journal | vauthors = Syriani E, Salvans C, Salvadó M, Morales M, Lorenzo L, Cazorla S, Gamez J | title = PFN1 mutations are also rare in the Catalan population with amyotrophic lateral sclerosis | journal = Journal of Neurology | volume = 261 | issue = 12 | pages = 2387-92 | date = December 2014 | pmid = 25249294 | doi = 10.1007/s00415-014-7501-x }}</ref><ref>{{cite journal | vauthors = Smith BN, Vance C, Scotter EL, Troakes C, Wong CH, Topp S, Maekawa S, King A, Mitchell JC, Lund K, Al-Chalabi A, Ticozzi N, Silani V, Sapp P, Brown RH, Landers JE, Al-Sarraj S, Shaw CE | display-authors = 6 | title = Novel mutations support a role for Profilin 1 in the pathogenesis of ALS | journal = Neurobiology of Aging | volume = 36 | issue = 3 | pages = 1602.e17-27 | date = March 2015 | pmid = 25499087 | pmc = 4357530 | doi = 10.1016/j.neurobiolaging.2014.10.032 }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: PFN1 profilin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5216| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
Profilin 1 has been shown to [[Protein-protein interaction|interact]] with:
* [[FMNL1]],<ref name = pmid10958683>{{cite journal | vauthors = Yayoshi-Yamamoto S, Taniuchi I, Watanabe T | title = FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages | journal = Mol. Cell. Biol. | volume = 20 | issue = 18 | pages = 6872–81 | date = September 2000 | pmid = 10958683 | pmc = 86228 | doi =  10.1128/mcb.20.18.6872-6881.2000}}</ref>
* [[MLLT4]]<ref name = pmid10922060>{{cite journal | vauthors = Boettner B, Govek EE, Cross J, Van Aelst L | title = The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 16 | pages = 9064–9 | date = August 2000 | pmid = 10922060 | pmc = 16822 | doi =  10.1073/pnas.97.16.9064}}</ref>
* [[Vasodilator-stimulated phosphoprotein]],<ref name = pmid10882740>{{cite journal | vauthors = Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S | title = Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin | journal = J. Biol. Chem. | volume = 275 | issue = 40 | pages = 30817–25 | date = October 2000 | pmid = 10882740 | doi = 10.1074/jbc.M005066200 }}</ref>
* [[WASF1]],<ref name = pmid9843499>{{cite journal | vauthors = Miki H, Suetsugu S, Takenawa T | title = WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac | journal = EMBO J. | volume = 17 | issue = 23 | pages = 6932–41 | date = December 1998 | pmid = 9843499 | pmc = 1171041 | doi = 10.1093/emboj/17.23.6932 }}</ref>  and
* [[WASL (gene)|WASL]].<ref name = pmid10867004>{{cite journal | vauthors = Mimuro H, Suzuki T, Suetsugu S, Miki H, Takenawa T, Sasakawa C | title = Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri | journal = J. Biol. Chem. | volume = 275 | issue = 37 | pages = 28893–901 | date = September 2000 | pmid = 10867004 | doi = 10.1074/jbc.M003882200 }}</ref><ref name = pmid9822597>{{cite journal | vauthors = Suetsugu S, Miki H, Takenawa T | title = The essential role of profilin in the assembly of actin for microspike formation | journal = EMBO J. | volume = 17 | issue = 22 | pages = 6516–26 | date = November 1998 | pmid = 9822597 | pmc = 1170999 | doi = 10.1093/emboj/17.22.6516 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Qualmann B, Kessels MM | title = Endocytosis and the cytoskeleton | journal = Int. Rev. Cytol. | volume = 220 | issue =  | pages = 93–144 | year = 2003 | pmid = 12224553 | doi = 10.1016/S0074-7696(02)20004-2 | isbn = 978-0-12-364624-8 | series = International Review of Cytology }}
| citations =
* {{cite journal | vauthors = Ampe C, Markey F, Lindberg U, Vandekerckhove J | title = The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence | journal = FEBS Lett. | volume = 228 | issue = 1 | pages = 17–21 | year = 1988 | pmid = 3342873 | doi = 10.1016/0014-5793(88)80575-1 }}
*{{cite journal | author=Qualmann B, Kessels MM |title=Endocytosis and the cytoskeleton. |journal=Int. Rev. Cytol. |volume=220 |issue=  |pages= 93-144 |year= 2003 |pmid= 12224553 |doi= }}
* {{cite journal | vauthors = Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W | title = Distinct biochemical characteristics of the two human profilin isoforms | journal = Eur. J. Biochem. | volume = 229 | issue = 3 | pages = 621–8 | year = 1995 | pmid = 7758455 | doi = 10.1111/j.1432-1033.1995.tb20506.x }}
*{{cite journal  | author=Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC |title=Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome. |journal=Am. J. Hum. Genet. |volume=46 |issue= 3 |pages= 559-67 |year= 1990 |pmid= 1968707 |doi= }}
* {{cite journal | vauthors = Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T | title = Construction of a human full-length cDNA bank | journal = Gene | volume = 150 | issue = 2 | pages = 243–50 | year = 1995 | pmid = 7821789 | doi = 10.1016/0378-1119(94)90433-2 }}
*{{cite journal | author=Ampe C, Markey F, Lindberg U, Vandekerckhove J |title=The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence. |journal=FEBS Lett. |volume=228 |issue= 1 |pages= 17-21 |year= 1988 |pmid= 3342873 |doi= }}
* {{cite journal | vauthors = Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L | title = Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern | journal = Biochemistry | volume = 32 | issue = 50 | pages = 13818–29 | year = 1994 | pmid = 8268157 | doi = 10.1021/bi00213a010 }}
*{{cite journal | author=Kwiatkowski DJ, Bruns GA |title=Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis. |journal=J. Biol. Chem. |volume=263 |issue= 12 |pages= 5910-5 |year= 1988 |pmid= 3356709 |doi= }}
* {{cite journal | vauthors = Schutt CE, Myslik JC, Rozycki MD, Goonesekere NC, Lindberg U | title = The structure of crystalline profilin-beta-actin | journal = Nature | volume = 365 | issue = 6449 | pages = 810–6 | year = 1993 | pmid = 8413665 | doi = 10.1038/365810a0 }}
*{{cite journal | author=Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W |title=Distinct biochemical characteristics of the two human profilin isoforms. |journal=Eur. J. Biochem. |volume=229 |issue= 3 |pages= 621-8 |year= 1995 |pmid= 7758455 |doi= }}
* {{cite journal | vauthors = Mahoney NM, Janmey PA, Almo SC | title = Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation | journal = Nat. Struct. Biol. | volume = 4 | issue = 11 | pages = 953–60 | year = 1997 | pmid = 9360613 | doi = 10.1038/nsb1197-953 }}
*{{cite journal | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi= }}
* {{cite journal | vauthors = Mammoto A, Sasaki T, Asakura T, Hotta I, Imamura H, Takahashi K, Matsuura Y, Shirao T, Takai Y | title = Interactions of drebrin and gephyrin with profilin | journal = Biochem. Biophys. Res. Commun. | volume = 243 | issue = 1 | pages = 86–9 | year = 1998 | pmid = 9473484 | doi = 10.1006/bbrc.1997.8068 }}
*{{cite journal | author=Metzler WJ, Constantine KL, Friedrichs MS, ''et al.'' |title=Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. |journal=Biochemistry |volume=32 |issue= 50 |pages= 13818-29 |year= 1994 |pmid= 8268157 |doi= }}
* {{cite journal | vauthors = Bhargavi V, Chari VB, Singh SS | title = Phosphatidylinositol 3-kinase binds to profilin through the p85 alpha subunit and regulates cytoskeletal assembly | journal = Biochem. Mol. Biol. Int. | volume = 46 | issue = 2 | pages = 241–8 | year = 1998 | pmid = 9801792 | doi = 10.1080/15216549800203752 }}
*{{cite journal | author=Schutt CE, Myslik JC, Rozycki MD, ''et al.'' |title=The structure of crystalline profilin-beta-actin. |journal=Nature |volume=365 |issue= 6449 |pages= 810-6 |year= 1993 |pmid= 8413665 |doi= 10.1038/365810a0 }}
* {{cite journal | vauthors = Suetsugu S, Miki H, Takenawa T | title = The essential role of profilin in the assembly of actin for microspike formation | journal = EMBO J. | volume = 17 | issue = 22 | pages = 6516–26 | year = 1999 | pmid = 9822597 | pmc = 1170999 | doi = 10.1093/emboj/17.22.6516 }}
*{{cite journal | author=Mahoney NM, Janmey PA, Almo SC |title=Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation. |journal=Nat. Struct. Biol. |volume=4 |issue= 11 |pages= 953-60 |year= 1997 |pmid= 9360613 |doi= }}
* {{cite journal | vauthors = Miki H, Suetsugu S, Takenawa T | title = WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac | journal = EMBO J. | volume = 17 | issue = 23 | pages = 6932–41 | year = 1999 | pmid = 9843499 | pmc = 1171041 | doi = 10.1093/emboj/17.23.6932 }}
*{{cite journal | author=Mammoto A, Sasaki T, Asakura T, ''et al.'' |title=Interactions of drebrin and gephyrin with profilin. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 86-9 |year= 1998 |pmid= 9473484 |doi= 10.1006/bbrc.1997.8068 }}
* {{cite journal | vauthors = Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC | title = Profilin binds proline-rich ligands in two distinct amide backbone orientations | journal = Nat. Struct. Biol. | volume = 6 | issue = 7 | pages = 666–71 | year = 1999 | pmid = 10404225 | doi = 10.1038/10722 }}
*{{cite journal | author=Bhargavi V, Chari VB, Singh SS |title=Phosphatidylinositol 3-kinase binds to profilin through the p85 alpha subunit and regulates cytoskeletal assembly. |journal=Biochem. Mol. Biol. Int. |volume=46 |issue= 2 |pages= 241-8 |year= 1998 |pmid= 9801792 |doi= }}
* {{cite journal | vauthors = Nunoi H, Yamazaki T, Tsuchiya H, Kato S, Malech HL, Matsuda I, Kanegasaki S | title = A heterozygous mutation of β-actin associated with neutrophil dysfunction and recurrent infection | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 96 | issue = 15 | pages = 8693–8 | year = 1999 | pmid = 10411937 | pmc = 17578 | doi = 10.1073/pnas.96.15.8693 }}
*{{cite journal | author=Suetsugu S, Miki H, Takenawa T |title=The essential role of profilin in the assembly of actin for microspike formation. |journal=EMBO J. |volume=17 |issue= 22 |pages= 6516-26 |year= 1999 |pmid= 9822597 |doi= 10.1093/emboj/17.22.6516 }}
* {{cite journal | vauthors = Murphy GA, Solski PA, Jillian SA, Pérez de la Ossa P, D'Eustachio P, Der CJ, Rush MG | title = Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth | journal = Oncogene | volume = 18 | issue = 26 | pages = 3831–45 | year = 1999 | pmid = 10445846 | doi = 10.1038/sj.onc.1202758 }}
*{{cite journal | author=Miki H, Suetsugu S, Takenawa T |title=WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac. |journal=EMBO J. |volume=17 |issue= 23 |pages= 6932-41 |year= 1999 |pmid= 9843499 |doi= 10.1093/emboj/17.23.6932 }}
* {{cite journal | vauthors = Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S | title = Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin | journal = J. Biol. Chem. | volume = 275 | issue = 40 | pages = 30817–25 | year = 2000 | pmid = 10882740 | doi = 10.1074/jbc.M005066200 }}
*{{cite journal | author=Mahoney NM, Rozwarski DA, Fedorov E, ''et al.'' |title=Profilin binds proline-rich ligands in two distinct amide backbone orientations. |journal=Nat. Struct. Biol. |volume=6 |issue= 7 |pages= 666-71 |year= 1999 |pmid= 10404225 |doi= 10.1038/10722 }}
* {{cite journal | vauthors = Boettner B, Govek EE, Cross J, Van Aelst L | title = The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 16 | pages = 9064–9 | year = 2000 | pmid = 10922060 | pmc = 16822 | doi = 10.1073/pnas.97.16.9064 }}
*{{cite journal | author=Nunoi H, Yamazaki T, Tsuchiya H, ''et al.'' |title=A heterozygous mutation of beta-actin associated with neutrophil dysfunction and recurrent infection. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 15 |pages= 8693-8 |year= 1999 |pmid= 10411937 |doi= }}
* {{cite journal | vauthors = Yayoshi-Yamamoto S, Taniuchi I, Watanabe T | title = FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages | journal = Mol. Cell. Biol. | volume = 20 | issue = 18 | pages = 6872–81 | year = 2000 | pmid = 10958683 | pmc = 86228 | doi = 10.1128/MCB.20.18.6872-6881.2000 }}
*{{cite journal | author=Murphy GA, Solski PA, Jillian SA, ''et al.'' |title=Cellular functions of TC10, a Rho family GTPase: regulation of morphology, signal transduction and cell growth. |journal=Oncogene |volume=18 |issue= 26 |pages= 3831-45 |year= 1999 |pmid= 10445846 |doi= 10.1038/sj.onc.1202758 }}
* {{cite journal | vauthors = Mellon MB, Frank BT, Fang KC | title = Mast cell alpha-chymase reduces IgE recognition of birch pollen profilin by cleaving antibody-binding epitopes | journal = J. Immunol. | volume = 168 | issue = 1 | pages = 290–7 | year = 2002 | pmid = 11751973 | doi = 10.4049/jimmunol.168.1.290 }}
*{{cite journal | author=Harbeck B, Hüttelmaier S, Schluter K, ''et al.'' |title=Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 30817-25 |year= 2000 |pmid= 10882740 |doi= 10.1074/jbc.M005066200 }}
*{{cite journal | author=Boettner B, Govek EE, Cross J, Van Aelst L |title=The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 16 |pages= 9064-9 |year= 2000 |pmid= 10922060 |doi= }}
*{{cite journal  | author=Yayoshi-Yamamoto S, Taniuchi I, Watanabe T |title=FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages. |journal=Mol. Cell. Biol. |volume=20 |issue= 18 |pages= 6872-81 |year= 2000 |pmid= 10958683 |doi=  }}
*{{cite journal  | author=Mellon MB, Frank BT, Fang KC |title=Mast cell alpha-chymase reduces IgE recognition of birch pollen profilin by cleaving antibody-binding epitopes. |journal=J. Immunol. |volume=168 |issue= 1 |pages= 290-7 |year= 2002 |pmid= 11751973 |doi=  }}
}}
{{refend}}
{{refend}}


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Revision as of 03:47, 5 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Wikidata
View/Edit Human

Profilin-1 is a protein that in humans is encoded by the PFN1 gene.[1][2]

Function

The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. Deletion of this gene is associated with Miller-Dieker syndrome.[3] Mutations in this gene may be a rare cause of amyotrophic lateral sclerosis, also called Lou Gehrig's disease.[4][5][6][7][8][9][10][11][12][13][14][15][16]

Interactions

Profilin 1 has been shown to interact with:

References

  1. ↑ Kwiatkowski DJ, Bruns GA (May 1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis". J Biol Chem. 263 (12): 5910–5. PMID 3356709.
  2. ↑ Kwiatkowski DJ, Aklog L, Ledbetter DH, Morton CC (April 1990). "Identification of the functional profilin gene, its localization to chromosome subband 17p13.3, and demonstration of its deletion in some patients with Miller-Dieker syndrome". Am J Hum Genet. 46 (3): 559–67. PMC 1683621. PMID 1968707.
  3. ↑ "Entrez Gene: PFN1 profilin 1".
  4. ↑ Wu CH, Fallini C, Ticozzi N, Keagle PJ, Sapp PC, Piotrowska K, et al. (August 2012). "Mutations in the profilin 1 gene cause familial amyotrophic lateral sclerosis". Nature. 488 (7412): 499–503. doi:10.1038/nature11280. PMC 3575525. PMID 22801503.
  5. ↑ Daoud H, Dobrzeniecka S, Camu W, Meininger V, Dupré N, Dion PA, Rouleau GA (April 2013). "Mutation analysis of PFN1 in familial amyotrophic lateral sclerosis patients". Neurobiology of Aging. 34 (4): 1311.e1–2. doi:10.1016/j.neurobiolaging.2012.09.001. PMID 23062600.
  6. ↑ Tiloca C, Ticozzi N, Pensato V, Corrado L, Del Bo R, Bertolin C, et al. (May 2013). "Screening of the PFN1 gene in sporadic amyotrophic lateral sclerosis and in frontotemporal dementia". Neurobiology of Aging. 34 (5): 1517.e9–10. doi:10.1016/j.neurobiolaging.2012.09.016. PMC 3548975. PMID 23063648.
  7. ↑ Ingre C, Landers JE, Rizik N, Volk AE, Akimoto C, Birve A, et al. (June 2013). "A novel phosphorylation site mutation in profilin 1 revealed in a large screen of US, Nordic, and German amyotrophic lateral sclerosis/frontotemporal dementia cohorts". Neurobiology of Aging. 34 (6): 1708.e1–6. doi:10.1016/j.neurobiolaging.2012.10.009. PMID 23141414.
  8. ↑ Lattante S, Le Ber I, Camuzat A, Brice A, Kabashi E (June 2013). "Mutations in the PFN1 gene are not a common cause in patients with amyotrophic lateral sclerosis and frontotemporal lobar degeneration in France". Neurobiology of Aging. 34 (6): 1709.e1–2. doi:10.1016/j.neurobiolaging.2012.10.026. PMID 23182804.
  9. ↑ Dillen L, Van Langenhove T, Engelborghs S, Vandenbulcke M, Sarafov S, Tournev I, et al. (June 2013). "Explorative genetic study of UBQLN2 and PFN1 in an extended Flanders-Belgian cohort of frontotemporal lobar degeneration patients". Neurobiology of Aging. 34 (6): 1711.e1–5. doi:10.1016/j.neurobiolaging.2012.12.007. PMID 23312802.
  10. ↑ Zou ZY, Sun Q, Liu MS, Li XG, Cui LY (June 2013). "Mutations in the profilin 1 gene are not common in amyotrophic lateral sclerosis of Chinese origin". Neurobiology of Aging. 34 (6): 1713.e5–6. doi:10.1016/j.neurobiolaging.2012.12.024. PMID 23357624.
  11. ↑ Chen Y, Zheng ZZ, Huang R, Chen K, Song W, Zhao B, et al. (July 2013). "PFN1 mutations are rare in Han Chinese populations with amyotrophic lateral sclerosis". Neurobiology of Aging. 34 (7): 1922.e1–5. doi:10.1016/j.neurobiolaging.2013.01.013. PMID 23428184.
  12. ↑ van Blitterswijk M, Baker MC, Bieniek KF, Knopman DS, Josephs KA, Boeve B, et al. (September 2013). "Profilin-1 mutations are rare in patients with amyotrophic lateral sclerosis and frontotemporal dementia". Amyotrophic Lateral Sclerosis & Frontotemporal Degeneration. 14 (5–6): 463–9. doi:10.3109/21678421.2013.787630. PMC 3923463. PMID 23634771.
  13. ↑ Yang S, Fifita JA, Williams KL, Warraich ST, Pamphlett R, Nicholson GA, et al. (September 2013). "Mutation analysis and immunopathological studies of PFN1 in familial and sporadic amyotrophic lateral sclerosis". Neurobiology of Aging. 34 (9): 2235.e7–10. doi:10.1016/j.neurobiolaging.2013.04.003. PMID 23635659.
  14. ↑ Fratta P, Charnock J, Collins T, Devoy A, Howard R, Malaspina A, et al. (May 2014). "Profilin1 E117G is a moderate risk factor for amyotrophic lateral sclerosis". Journal of Neurology, Neurosurgery, and Psychiatry. 85 (5): 506–8. doi:10.1136/jnnp-2013-306761. PMC 3995330. PMID 24309268.
  15. ↑ Syriani E, Salvans C, Salvadó M, Morales M, Lorenzo L, Cazorla S, Gamez J (December 2014). "PFN1 mutations are also rare in the Catalan population with amyotrophic lateral sclerosis". Journal of Neurology. 261 (12): 2387–92. doi:10.1007/s00415-014-7501-x. PMID 25249294.
  16. ↑ Smith BN, Vance C, Scotter EL, Troakes C, Wong CH, Topp S, et al. (March 2015). "Novel mutations support a role for Profilin 1 in the pathogenesis of ALS". Neurobiology of Aging. 36 (3): 1602.e17–27. doi:10.1016/j.neurobiolaging.2014.10.032. PMC 4357530. PMID 25499087.
  17. ↑ Yayoshi-Yamamoto S, Taniuchi I, Watanabe T (September 2000). "FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages". Mol. Cell. Biol. 20 (18): 6872–81. doi:10.1128/mcb.20.18.6872-6881.2000. PMC 86228. PMID 10958683.
  18. ↑ Boettner B, Govek EE, Cross J, Van Aelst L (August 2000). "The junctional multidomain protein AF-6 is a binding partner of the Rap1A GTPase and associates with the actin cytoskeletal regulator profilin". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9064–9. doi:10.1073/pnas.97.16.9064. PMC 16822. PMID 10922060.
  19. ↑ Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
  20. ↑ Miki H, Suetsugu S, Takenawa T (December 1998). "WAVE, a novel WASP-family protein involved in actin reorganization induced by Rac". EMBO J. 17 (23): 6932–41. doi:10.1093/emboj/17.23.6932. PMC 1171041. PMID 9843499.
  21. ↑ Mimuro H, Suzuki T, Suetsugu S, Miki H, Takenawa T, Sasakawa C (September 2000). "Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri". J. Biol. Chem. 275 (37): 28893–901. doi:10.1074/jbc.M003882200. PMID 10867004.
  22. ↑ Suetsugu S, Miki H, Takenawa T (November 1998). "The essential role of profilin in the assembly of actin for microspike formation". EMBO J. 17 (22): 6516–26. doi:10.1093/emboj/17.22.6516. PMC 1170999. PMID 9822597.

Further reading


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