# VPS25

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**Vacuolar protein-sorting-associated protein 25** is a [protein](/source/Protein) that in humans is encoded by the *VPS25* [gene](/source/Gene).[1][2]

It is a component of the endosome-associated [complex](/source/Protein_complex) [ESCRT-II](/source/ESCRT-II) ([Endosomal](/source/Endosomal) Sorting Complexes Required for Transport protein II). ESCRT (ESCRT-I, -II, -III) complexes orchestrate efficient sorting of [ubiquitinated](/source/Ubiquitinated) [transmembrane receptors](/source/Transmembrane_receptor) to [lysosomes](/source/Lysosome) via [multivesicular bodies](/source/Multivesicular_bodies) (MVBs).[3] ESCRT-II recruits the transport machinery for protein sorting at MVB.[4] In addition, the [human](/source/Homo_sapiens) ESCRT-II has been shown to form a complex with [RNA polymerase II](/source/RNA_polymerase_II) elongation factor [ELL](/source/ELL_(gene)) in order to exert [transcriptional](/source/Transcription_(genetics)) control activity. ESCRT-II transiently associates with the [endosomal membrane](/source/Endosomal_membrane) and thereby initiates the formation of ESCRT-III, a membrane-associated [protein complex](/source/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](/source/VPS22) and the [C-terminal](/source/C-terminal) region of [vps36](/source/VPS36). The [crystal structure](/source/Crystal_structure) of vps25 revealed two winged-helix domains, the [N-terminal](/source/N-terminal) domain of vps25 interacting with vps22 and vps36.[6]

## References

1. Yorikawa C, Shibata H, Waguri S, Hatta K, Horii M, Katoh K, Kobayashi T, Uchiyama Y, Maki M (Mar 2005). "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. [doi:10.1042/BJ20041227](https://doi.org/10.1042/BJ20041227). [PMC 1134928](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1134928). [PMID 15511219](https://pubmed.ncbi.nlm.nih.gov/15511219)

1. ["Entrez Gene: VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae)"](https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=84313)

1. Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL (January 2007). "Structural insight into the ESCRT-I/-II link and its role in MVB trafficking". *EMBO J.*. **26** (2): 600–12. [doi:10.1038/sj.emboj.7601501](https://doi.org/10.1038/sj.emboj.7601501). [PMC 1783442](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1783442). [PMID 17215868](https://pubmed.ncbi.nlm.nih.gov/17215868)

1. Teo H, Perisic O, Gonzalez B, Williams RL (October 2004). "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. [doi:10.1016/j.devcel.2004.09.003](https://doi.org/10.1016/j.devcel.2004.09.003). [PMID 15469844](https://pubmed.ncbi.nlm.nih.gov/15469844)

1. Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD (August 2002). "Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body". *Dev. Cell*. **3** (2): 283–9. [doi:10.1016/S1534-5807(02)00219-8](https://doi.org/10.1016/S1534-5807(02)00219-8). [PMID 12194858](https://pubmed.ncbi.nlm.nih.gov/12194858)

1. Wernimont AK, Weissenhorn W (December 2004). "Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II". *BMC Struct. Biol.*. **4** (1): 10. [doi:10.1186/1472-6807-4-10](https://doi.org/10.1186/1472-6807-4-10). [PMC 539351](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC539351). [PMID 15579210](https://pubmed.ncbi.nlm.nih.gov/15579210)

## Further reading

- Kamura T, Burian D, Khalili H, etal (2001). "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. [doi:10.1074/jbc.M010142200](https://doi.org/10.1074/jbc.M010142200). [PMID 11278625](https://pubmed.ncbi.nlm.nih.gov/11278625)
- Strausberg RL, Feingold EA, Grouse LH, etal (2003). "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. [Bibcode:2002PNAS...9916899M](https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M). [doi:10.1073/pnas.242603899](https://doi.org/10.1073/pnas.242603899). [PMC 139241](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241). [PMID 12477932](https://pubmed.ncbi.nlm.nih.gov/12477932)
- von Schwedler UK, Stuchell M, Müller B, etal (2003). "The protein network of HIV budding.". *Cell*. **114** (6): 701–13. [doi:10.1016/S0092-8674(03)00714-1](https://doi.org/10.1016/S0092-8674(03)00714-1). [PMID 14505570](https://pubmed.ncbi.nlm.nih.gov/14505570). [S2CID 16894972](https://api.semanticscholar.org/CorpusID:16894972)
- Martin-Serrano J, Yarovoy A, Perez-Caballero D, etal (2003). "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. [Bibcode:2003PNAS..10012414M](https://ui.adsabs.harvard.edu/abs/2003PNAS..10012414M). [doi:10.1073/pnas.2133846100](https://doi.org/10.1073/pnas.2133846100). [PMC 218772](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC218772). [PMID 14519844](https://pubmed.ncbi.nlm.nih.gov/14519844)
- Sharma M, Pampinella F, Nemes C, etal (2004). "Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes.". *J. Cell Biol.*. **164** (6): 923–33. [doi:10.1083/jcb.200312018](https://doi.org/10.1083/jcb.200312018). [PMC 2172283](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172283). [PMID 15007060](https://pubmed.ncbi.nlm.nih.gov/15007060)
- Gerhard DS, Wagner L, Feingold EA, etal (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". *Genome Res.*. **14** (10B): 2121–7. [doi:10.1101/gr.2596504](https://doi.org/10.1101/gr.2596504). [PMC 528928](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC528928). [PMID 15489334](https://pubmed.ncbi.nlm.nih.gov/15489334)
- Rual JF, Venkatesan K, Hao T, etal (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". *Nature*. **437** (7062): 1173–8. [Bibcode:2005Natur.437.1173R](https://ui.adsabs.harvard.edu/abs/2005Natur.437.1173R). [doi:10.1038/nature04209](https://doi.org/10.1038/nature04209). [PMID 16189514](https://pubmed.ncbi.nlm.nih.gov/16189514). [S2CID 4427026](https://api.semanticscholar.org/CorpusID:4427026)
- Bowers K, Piper SC, Edeling MA, etal (2006). "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. [doi:10.1074/jbc.M508632200](https://doi.org/10.1074/jbc.M508632200). [PMID 16371348](https://pubmed.ncbi.nlm.nih.gov/16371348)

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Adapted from the Wikipedia article [VPS25](https://en.wikipedia.org/wiki/VPS25) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/VPS25?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.