VPS25
{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
{{Infobox protein family
| Symbol = ESCRT-II
| Name = ESCRT-II complex subunit
| image = PDB 1xb4 EBI.jpg
| width =
| caption = crystal structure of subunit vps25 of the endosomal trafficking complex escrt-ii
| Pfam = PF05871
| Pfam_clan =
| InterPro = IPR008570
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
Vacuolar protein-sorting-associated protein 25 is a protein that in humans is encoded by the VPS25 gene.{{cite journal | vauthors = Yorikawa C, Shibata H, Waguri S, Hatta K, Horii M, Katoh K, Kobayashi T, Uchiyama Y, Maki M | title = Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting | journal = Biochem J | volume = 387 | issue = Pt 1 | pages = 17–26 |date=Mar 2005 | pmid = 15511219 | pmc = 1134928 | doi = 10.1042/BJ20041227 }}{{cite web | title = Entrez Gene: VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84313}}
It is a component of the endosome-associated complex ESCRT-II (Endosomal Sorting Complexes Required for Transport protein II). ESCRT (ESCRT-I, -II, -III) complexes orchestrate efficient sorting of ubiquitinated transmembrane receptors to lysosomes via multivesicular bodies (MVBs).{{cite journal | vauthors = Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL | title = Structural insight into the ESCRT-I/-II link and its role in MVB trafficking | journal = EMBO J. | volume = 26 | issue = 2 | pages = 600–12 |date=January 2007 | pmid = 17215868 | pmc = 1783442 | doi = 10.1038/sj.emboj.7601501 }} ESCRT-II recruits the transport machinery for protein sorting at MVB.{{cite journal | vauthors = Teo H, Perisic O, Gonzalez B, Williams RL | title = ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes | journal = Dev. Cell | volume = 7 | issue = 4 | pages = 559–69 |date=October 2004 | pmid = 15469844 | doi = 10.1016/j.devcel.2004.09.003 | doi-access = free }} In addition, the human ESCRT-II has been shown to form a complex with RNA polymerase II elongation factor ELL in order to exert transcriptional control activity. ESCRT-II transiently associates with the endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo.{{cite journal | vauthors = Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD | title = Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body | journal = Dev. Cell | volume = 3 | issue = 2 | pages = 283–9 |date=August 2002 | pmid = 12194858 | doi = 10.1016/S1534-5807(02)00219-8| doi-access = free }}
ESCRT-II is a trilobal complex composed of two copies of vps25, one copy of vps22 and the C-terminal region of vps36. The crystal structure of vps25 revealed two winged-helix domains, the N-terminal domain of vps25 interacting with vps22 and vps36.{{cite journal | vauthors = Wernimont AK, Weissenhorn W | title = Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II | journal = BMC Struct. Biol. | volume = 4 | issue = 1 | pages = 10 |date=December 2004 | pmid = 15579210 | pmc = 539351 | doi = 10.1186/1472-6807-4-10 | doi-access = free }}
References
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Further reading
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- {{cite journal |vauthors=Kamura T, Burian D, Khalili H, etal |title=Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a role for yeast EAP-like proteins in regulation of gene expression by glucose. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16528–33 |year= 2001 |pmid= 11278625 |doi= 10.1074/jbc.M010142200 |doi-access= free }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 |bibcode=2002PNAS...9916899M |doi-access=free }}
- {{cite journal |vauthors=von Schwedler UK, Stuchell M, Müller B, etal |title=The protein network of HIV budding. |journal=Cell |volume=114 |issue= 6 |pages= 701–13 |year= 2003 |pmid= 14505570 |doi=10.1016/S0092-8674(03)00714-1 |s2cid=16894972 |doi-access=free }}
- {{cite journal |vauthors=Martin-Serrano J, Yarovoy A, Perez-Caballero D, etal |title=Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 21 |pages= 12414–9 |year= 2003 |pmid= 14519844 |doi= 10.1073/pnas.2133846100 | pmc=218772 |bibcode=2003PNAS..10012414M |doi-access=free }}
- {{cite journal |vauthors=Sharma M, Pampinella F, Nemes C, etal |title=Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes. |journal=J. Cell Biol. |volume=164 |issue= 6 |pages= 923–33 |year= 2004 |pmid= 15007060 |doi= 10.1083/jcb.200312018 | pmc=2172283 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |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 }}
- {{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R |s2cid=4427026 }}
- {{cite journal |vauthors=Bowers K, Piper SC, Edeling MA, etal |title=Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII. |journal=J. Biol. Chem. |volume=281 |issue= 8 |pages= 5094–105 |year= 2006 |pmid= 16371348 |doi= 10.1074/jbc.M508632200 |doi-access= free }}
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{{InterPro content|IPR008570}}
{{gene-17-stub}}