Biology:VPS25
 Generic protein structure example |
| ESCRT-II complex subunit | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of subunit vps25 of the endosomal trafficking complex escrt-ii | |||||||||
| Identifiers | |||||||||
| Symbol | ESCRT-II | ||||||||
| Pfam | PF05871 | ||||||||
| InterPro | IPR008570 | ||||||||
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Vacuolar protein-sorting-associated protein 25 is a protein that in humans is encoded by the VPS25 gene.[1][2]
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).[3] ESCRT-II recruits the transport machinery for protein sorting at MVB.[4] 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.[5]
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.[6]
References
- ↑ "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting". Biochem J 387 (Pt 1): 17–26. Mar 2005. doi:10.1042/BJ20041227. PMID 15511219.
- ↑ "Entrez Gene: VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84313.
- ↑ "Structural insight into the ESCRT-I/-II link and its role in MVB trafficking". EMBO J. 26 (2): 600–12. January 2007. doi:10.1038/sj.emboj.7601501. PMID 17215868.
- ↑ "ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes". Dev. Cell 7 (4): 559–69. October 2004. doi:10.1016/j.devcel.2004.09.003. PMID 15469844.
- ↑ "Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body". Dev. Cell 3 (2): 283–9. August 2002. doi:10.1016/S1534-5807(02)00219-8. PMID 12194858.
- ↑ "Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II". BMC Struct. Biol. 4 (1): 10. December 2004. doi:10.1186/1472-6807-4-10. PMID 15579210.
Further reading
- "Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a role for yeast EAP-like proteins in regulation of gene expression by glucose.". J. Biol. Chem. 276 (19): 16528–33. 2001. doi:10.1074/jbc.M010142200. PMID 11278625.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "The protein network of HIV budding.". Cell 114 (6): 701–13. 2003. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570.
- "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins.". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. 2003. doi:10.1073/pnas.2133846100. PMID 14519844. Bibcode: 2003PNAS..10012414M.
- "Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes.". J. Cell Biol. 164 (6): 923–33. 2004. doi:10.1083/jcb.200312018. PMID 15007060.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII.". J. Biol. Chem. 281 (8): 5094–105. 2006. doi:10.1074/jbc.M508632200. PMID 16371348.
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