FBXO11: Difference between revisions

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{{Underlinked|date=May 2016}}
{{Infobox_gene}}
'''F-box only protein 11''' is a [[protein]] that in humans is encoded by the ''FBXO11'' [[gene]].<ref name="pmid10531035">{{cite journal | vauthors = Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M | title = Identification of a family of human F-box proteins | journal = Current Biology | volume = 9 | issue = 20 | pages = 1177–9 | date = October 1999 | pmid = 10531035 | pmc =  | doi = 10.1016/S0960-9822(00)80020-2 }}</ref><ref name="pmid16487488">{{cite journal | vauthors = Cook JR, Lee JH, Yang ZH, Krause CD, Herth N, Hoffmann R, Pestka S | title = FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues | journal = Biochemical and Biophysical Research Communications | volume = 342 | issue = 2 | pages = 472–81 | date = April 2006 | pmid = 16487488 | pmc =  | doi = 10.1016/j.bbrc.2006.01.167 }}</ref><ref name="pmid18162545">{{cite journal | vauthors = Lee MJ, Pal K, Tasaki T, Roy S, Jiang Y, An JY, Banerjee R, Kwon YT | title = Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 1 | pages = 100–5 | date = January 2008 | pmid = 18162545 | pmc = 2224166 | doi = 10.1073/pnas.0708465105 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FBXO11 F-box protein 11| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80204| access-date = }}</ref>
 
== Function ==
 
This gene encodes a member of the [[F-box protein]] family which is characterized by an approximately 40 amino acid [[sequence motif|motif]], the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in [[phosphorylation]]-dependent [[ubiquitination]]. The F-box proteins are divided into 3 classes: Fbws containing [[WD-40 domain]]s, Fbls containing [[leucine-rich repeat]]s, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez" />
 
FBXO11 is conserved from [[nematode]]s to mammals, and both human FBXO11 and its worm ortholog (DRE-1) form functional SCF [[ubiquitin ligase]] complexes. By binding to and mediating the degradation of its substrate proteins, FBXO11 plays important roles in regulating cell cycle regulation, [[tumorigenesis]], and tumor cell [[metastasis]]. Well established targets of FBXO11 include [[BCL6]],<ref name="Duan_2012">{{cite journal | vauthors = Duan S, Cermak L, Pagan JK, Rossi M, Martinengo C, di Celle PF, Chapuy B, Shipp M, Chiarle R, Pagano M | title = FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas | journal = Nature | volume = 481 | issue = 7379 | pages = 90–3 | date = January 2012 | pmid = 22113614 | pmc = 3344385 | doi = 10.1038/nature10688 }}</ref><ref name="pmid23478445">{{cite journal | vauthors = Abbas T, Mueller AC, Shibata E, Keaton M, Rossi M, Dutta A | title = CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration | journal = Molecular Cell | volume = 49 | issue = 6 | pages = 1147–58 | date = March 2013 | pmid = 23478445 | pmc = 3615078 | doi = 10.1016/j.molcel.2013.02.003 }}</ref><ref name="Rossi_2013">{{cite journal | vauthors = Rossi M, Duan S, Jeong YT, Horn M, Saraf A, Florens L, Washburn MP, Antebi A, Pagano M | title = Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase | journal = Molecular Cell | volume = 49 | issue = 6 | pages = 1159–66 | date = March 2013 | pmid = 23478441 | pmc = 3624904 | doi = 10.1016/j.molcel.2013.02.004 }}</ref> and [[SNAI1|Snail]].<ref name="Zheng_2014">{{cite journal | vauthors = Zheng H, Shen M, Zha YL, Li W, Wei Y, Blanco MA, Ren G, Zhou T, Storz P, Wang HY, Kang Y | title = PKD1 phosphorylation-dependent degradation of SNAIL by SCF-FBXO11 regulates epithelial-mesenchymal transition and metastasis | journal = Cancer Cell | volume = 26 | issue = 3 | pages = 358–373 | date = September 2014 | pmid = 25203322 | pmc = 4159622 | doi = 10.1016/j.ccr.2014.07.022 }}</ref>


{{Infobox_gene}}
== Clinical significance ==
'''F-box only protein 11''' is a [[protein]] that in humans is encoded by the ''FBXO11'' [[gene]].<ref name="pmid10531035">{{cite journal | vauthors = Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M | title = Identification of a family of human F-box proteins | journal = Curr Biol | volume = 9 | issue = 20 | pages = 1177–9 |date=Dec 1999 | pmid = 10531035 | pmc =  | doi = 10.1016/S0960-9822(00)80020-2 }}</ref><ref name="pmid16487488">{{cite journal | vauthors = Cook JR, Lee JH, Yang ZH, Krause CD, Herth N, Hoffmann R, Pestka S | title = FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues | journal = Biochem Biophys Res Commun | volume = 342 | issue = 2 | pages = 472–81 |date=Feb 2006 | pmid = 16487488 | pmc =  | doi = 10.1016/j.bbrc.2006.01.167 }}</ref><ref name="pmid18162545">{{cite journal | vauthors = Lee MJ, Pal K, Tasaki T, Roy S, Jiang Y, An JY, Banerjee R, Kwon YT | title = Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway | journal = Proc Natl Acad Sci U S A | volume = 105 | issue = 1 | pages = 100–5 |date=Jan 2008 | pmid = 18162545 | pmc = 2224166 | doi = 10.1073/pnas.0708465105 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FBXO11 F-box protein 11| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=80204| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Inactivation of FBXO11-mediated BCL6 degradation has been shown to contribute to abnormal germinal-center formation and tumorigenesis.<ref name="Schneider_2016">{{cite journal | vauthors = Schneider C, Kon N, Amadori L, Shen Q, Schwartz FH, Tischler B, Bossennec M, Dominguez-Sola D, Bhagat G, Gu W, Basso K, Dalla-Favera R | title = FBXO11 inactivation leads to abnormal germinal-center formation and lymphoproliferative disease | journal = Blood | volume = 128 | issue = 5 | pages = 660–6 | date = August 2016 | pmid = 27166359 | doi = 10.1182/blood-2015-11-684357 }}</ref> The ''Caenorhabditis elegans'' DRE-1/FBXO11 was reported to target the conserved transcription factor BLMP-1 for proteasomal degradation, and thereby regulates developmental timing and maturation.<ref>Dev Cell. 2014 Mar 31;28(6):697-710. doi: 10.1016/j.devcel.2014.01.028. DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans developmental timing and maturation. Horn M, Geisen C, Cermak L, Becker B, Nakamura S, Klein C, Pagano M, Antebi A.</ref>  The gene encoding FBXO11 was found to be deleted or mutated in multiple diffuse large B cell lymphoma (DLBCL) cell lines, and this inactivation of FBXO11 contributes to increased levels BCL6 and subsequently DLBCL pathogenesis.<ref name="Duan_2012" /> FBXO11 mutations were also identified in other human cancers, such as colon, lung, ovary, and head and neck tumors. In mice, a homozygous mutation of FBXO11 results in [[cleft palate]] defects, facial clefting, and [[perinatal lethality]]. Moreover, [[haploinsufficient]] mutant alleles cause [[otitis media]], a disorder that affects approximately 15% of children.<ref name="Hardisty-Hughes_2006">{{cite journal | vauthors = Hardisty-Hughes RE, Tateossian H, Morse SA, Romero MR, Middleton A, Tymowska-Lalanne Z, Hunter AJ, Cheeseman M, Brown SD | title = A mutation in the F-box gene, Fbxo11, causes otitis media in the Jeff mouse | journal = Human Molecular Genetics | volume = 15 | issue = 22 | pages = 3273–9 | date = November 2006 | pmid = 17035249 | doi = 10.1093/hmg/ddl403 }}</ref>
{{PBB_Summary
| section_title =  
| summary_text = This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez" />
}}


==References==
== References ==
{{reflist}}
{{reflist|32em}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|32em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = January 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
| citations =
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = October 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
* {{cite journal | vauthors = Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper JW | title = A family of mammalian F-box proteins | journal = Current Biology | volume = 9 | issue = 20 | pages = 1180–2 | date = October 1999 | pmid = 10531037 | doi = 10.1016/S0960-9822(00)80021-4 }}
*{{cite journal | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
* {{cite journal | vauthors = Le Poole IC, Sarangarajan R, Zhao Y, Stennett LS, Brown TL, Sheth P, Miki T, Boissy RE | title = 'VIT1', a novel gene associated with vitiligo | journal = Pigment Cell Research | volume = 14 | issue = 6 | pages = 475–84 | date = December 2001 | pmid = 11775060 | pmc = 1747534 | doi = 10.1034/j.1600-0749.2001.140608.x }}
*{{cite journal | vauthors=Winston JT, Koepp DM, Zhu C |title=A family of mammalian F-box proteins |journal=Curr. Biol. |volume=9 |issue= 20 |pages= 1180–2 |year= 1999 |pmid= 10531037 |doi= 10.1016/S0960-9822(00)80021-4 |display-authors=etal}}
* {{cite journal | vauthors = Segade F, Daly KA, Allred D, Hicks PJ, Cox M, Brown M, Hardisty-Hughes RE, Brown SD, Rich SS, Bowden DW | title = Association of the FBXO11 gene with chronic otitis media with effusion and recurrent otitis media: the Minnesota COME/ROM Family Study | journal = Archives of Otolaryngology–Head & Neck Surgery | volume = 132 | issue = 7 | pages = 729–33 | date = July 2006 | pmid = 16847180 | pmc = 1904347 | doi = 10.1001/archotol.132.7.729 }}
*{{cite journal | vauthors=Le Poole IC, Sarangarajan R, Zhao Y |title='VIT1', A Novel Gene Associated with Vitiligo |journal=Pigment Cell Res. |volume=14 |issue= 6 |pages= 475–84 |year= 2002 |pmid= 11775060 |doi= 10.1034/j.1600-0749.2001.140608.x| pmc=1747534  |display-authors=etal}}
* {{cite journal | vauthors = Abida WM, Nikolaev A, Zhao W, Zhang W, Gu W | title = FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity | journal = The Journal of Biological Chemistry | volume = 282 | issue = 3 | pages = 1797–804 | date = January 2007 | pmid = 17098746 | doi = 10.1074/jbc.M609001200 | pmc = 3690493 }}
*{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |display-authors=etal}}
*{{cite journal  | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 |display-authors=etal}}
*{{cite journal  | vauthors=Segade F, Daly KA, Allred D |title=Association of the FBXO11 gene with COME/ROM in the Minnesota COME/ROM Family Study |journal=Arch. Otolaryngol. Head Neck Surg. |volume=132 |issue= 7 |pages= 729–33 |year= 2006 |pmid= 16847180 |doi= 10.1001/archotol.132.7.729 | pmc=1904347 |display-authors=etal}}
*{{cite journal | vauthors=Abida WM, Nikolaev A, Zhao W |title=FBXO11 promotes the Neddylation of p53 and inhibits its transcriptional activity |journal=J. Biol. Chem. |volume=282 |issue= 3 |pages= 1797–804 |year= 2007 |pmid= 17098746 |doi= 10.1074/jbc.M609001200 |display-authors=etal}}
}}
{{refend}}
{{refend}}
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Latest revision as of 23:13, 10 January 2019

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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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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

F-box only protein 11 is a protein that in humans is encoded by the FBXO11 gene.[1][2][3][4]

Function

This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene.[4]

FBXO11 is conserved from nematodes to mammals, and both human FBXO11 and its worm ortholog (DRE-1) form functional SCF ubiquitin ligase complexes. By binding to and mediating the degradation of its substrate proteins, FBXO11 plays important roles in regulating cell cycle regulation, tumorigenesis, and tumor cell metastasis. Well established targets of FBXO11 include BCL6,[5][6][7] and Snail.[8]

Clinical significance

Inactivation of FBXO11-mediated BCL6 degradation has been shown to contribute to abnormal germinal-center formation and tumorigenesis.[9] The Caenorhabditis elegans DRE-1/FBXO11 was reported to target the conserved transcription factor BLMP-1 for proteasomal degradation, and thereby regulates developmental timing and maturation.[10] The gene encoding FBXO11 was found to be deleted or mutated in multiple diffuse large B cell lymphoma (DLBCL) cell lines, and this inactivation of FBXO11 contributes to increased levels BCL6 and subsequently DLBCL pathogenesis.[5] FBXO11 mutations were also identified in other human cancers, such as colon, lung, ovary, and head and neck tumors. In mice, a homozygous mutation of FBXO11 results in cleft palate defects, facial clefting, and perinatal lethality. Moreover, haploinsufficient mutant alleles cause otitis media, a disorder that affects approximately 15% of children.[11]

References

  1. ↑ Cenciarelli C, Chiaur DS, Guardavaccaro D, Parks W, Vidal M, Pagano M (October 1999). "Identification of a family of human F-box proteins". Current Biology. 9 (20): 1177–9. doi:10.1016/S0960-9822(00)80020-2. PMID 10531035.
  2. ↑ Cook JR, Lee JH, Yang ZH, Krause CD, Herth N, Hoffmann R, Pestka S (April 2006). "FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues". Biochemical and Biophysical Research Communications. 342 (2): 472–81. doi:10.1016/j.bbrc.2006.01.167. PMID 16487488.
  3. ↑ Lee MJ, Pal K, Tasaki T, Roy S, Jiang Y, An JY, Banerjee R, Kwon YT (January 2008). "Synthetic heterovalent inhibitors targeting recognition E3 components of the N-end rule pathway". Proceedings of the National Academy of Sciences of the United States of America. 105 (1): 100–5. doi:10.1073/pnas.0708465105. PMC 2224166. PMID 18162545.
  4. ↑ 4.0 4.1 "Entrez Gene: FBXO11 F-box protein 11".
  5. ↑ 5.0 5.1 Duan S, Cermak L, Pagan JK, Rossi M, Martinengo C, di Celle PF, Chapuy B, Shipp M, Chiarle R, Pagano M (January 2012). "FBXO11 targets BCL6 for degradation and is inactivated in diffuse large B-cell lymphomas". Nature. 481 (7379): 90–3. doi:10.1038/nature10688. PMC 3344385. PMID 22113614.
  6. ↑ Abbas T, Mueller AC, Shibata E, Keaton M, Rossi M, Dutta A (March 2013). "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration". Molecular Cell. 49 (6): 1147–58. doi:10.1016/j.molcel.2013.02.003. PMC 3615078. PMID 23478445.
  7. ↑ Rossi M, Duan S, Jeong YT, Horn M, Saraf A, Florens L, Washburn MP, Antebi A, Pagano M (March 2013). "Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase". Molecular Cell. 49 (6): 1159–66. doi:10.1016/j.molcel.2013.02.004. PMC 3624904. PMID 23478441.
  8. ↑ Zheng H, Shen M, Zha YL, Li W, Wei Y, Blanco MA, Ren G, Zhou T, Storz P, Wang HY, Kang Y (September 2014). "PKD1 phosphorylation-dependent degradation of SNAIL by SCF-FBXO11 regulates epithelial-mesenchymal transition and metastasis". Cancer Cell. 26 (3): 358–373. doi:10.1016/j.ccr.2014.07.022. PMC 4159622. PMID 25203322.
  9. ↑ Schneider C, Kon N, Amadori L, Shen Q, Schwartz FH, Tischler B, Bossennec M, Dominguez-Sola D, Bhagat G, Gu W, Basso K, Dalla-Favera R (August 2016). "FBXO11 inactivation leads to abnormal germinal-center formation and lymphoproliferative disease". Blood. 128 (5): 660–6. doi:10.1182/blood-2015-11-684357. PMID 27166359.
  10. ↑ Dev Cell. 2014 Mar 31;28(6):697-710. doi: 10.1016/j.devcel.2014.01.028. DRE-1/FBXO11-dependent degradation of BLMP-1/BLIMP-1 governs C. elegans developmental timing and maturation. Horn M, Geisen C, Cermak L, Becker B, Nakamura S, Klein C, Pagano M, Antebi A.
  11. ↑ Hardisty-Hughes RE, Tateossian H, Morse SA, Romero MR, Middleton A, Tymowska-Lalanne Z, Hunter AJ, Cheeseman M, Brown SD (November 2006). "A mutation in the F-box gene, Fbxo11, causes otitis media in the Jeff mouse". Human Molecular Genetics. 15 (22): 3273–9. doi:10.1093/hmg/ddl403. PMID 17035249.

Further reading


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