VPS18
Vacuolar protein sorting-associated protein 18 homolog is a protein that in humans is encoded by the VPS18 gene.[1][2][3]
Function
Vesicle mediated protein sorting plays an important role in segregation of intracellular molecules into distinct organelles. Genetic studies in yeast have identified more than 40 vacuolar protein sorting (VPS) genes involved in vesicle transport to vacuoles. This gene encodes the human homolog of yeast class C Vps18 protein. The mammalian class C Vps proteins are predominantly associated with late endosomes/lysosomes, and like their yeast counterparts, may mediate vesicle trafficking steps in the endosome/lysosome pathway.[3]
Interactions
VPS18 has been shown to interact with VPS11[4] and STX7.[4]
References
- ↑ Huizing M, Didier A, Walenta J, Anikster Y, Gahl WA, Krämer H (March 2001). "Molecular cloning and characterization of human VPS18, VPS 11, VPS16, and VPS33". Gene 264 (2): 241–7. doi:10.1016/S0378-1119(01)00333-X. PMID 11250079.
- ↑ Yogosawa S, Hatakeyama S, Nakayama KI, Miyoshi H, Kohsaka S, Akazawa C (Dec 2005). "Ubiquitylation and degradation of serum-inducible kinase by hVPS18, a RING-H2 type ubiquitin ligase". J Biol Chem 280 (50): 41619–27. doi:10.1074/jbc.M508397200. PMID 16203730.
- 1 2 "Entrez Gene: VPS18 vacuolar protein sorting 18 homolog (S. cerevisiae)".
- 1 2 Kim BY, Krämer H, Yamamoto A, Kominami E, Kohsaka S, Akazawa C (August 2001). "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7". J. Biol. Chem. 276 (31): 29393–402. doi:10.1074/jbc.M101778200. PMID 11382755.
Further reading
- Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O (2000). "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 7 (2): 143–50. doi:10.1093/dnares/7.2.143. PMID 10819331.
- Kim BY, Krämer H, Yamamoto A, Kominami E, Kohsaka S, Akazawa C (2001). "Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7.". J. Biol. Chem. 276 (31): 29393–402. doi:10.1074/jbc.M101778200. PMID 11382755.
- Kim BY, Ueda M, Kominami E, Akagawa K, Kohsaka S, Akazawa C (2004). "Identification of mouse Vps16 and biochemical characterization of mammalian class C Vps complex.". Biochem. Biophys. Res. Commun. 311 (3): 577–82. doi:10.1016/j.bbrc.2003.10.030. PMID 14623309.
- Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Yogosawa S, Kawasaki M, Wakatsuki S, Kominami E, Shiba Y, Nakayama K, Kohsaka S, Akazawa C (2006). "Monoubiquitylation of GGA3 by hVPS18 regulates its ubiquitin-binding ability.". Biochem. Biophys. Res. Commun. 350 (1): 82–90. doi:10.1016/j.bbrc.2006.09.013. PMID 16996030.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
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