CHMP6 explained

Charged multivesicular body protein 6 is a protein that in humans is encoded by the CHMP6 gene.^{[1] [2] [3]} It is one of charged multivesicular body proteins and a part of endosomal sorting complexes required for transport-III (ESCRT-III) complex.

See also

• Multivesicular body

Further reading

• Maruyama K, Sugano S . Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. . Gene . 138 . 1–2 . 171–4 . 1994 . 8125298 . 10.1016/0378-1119(94)90802-8 .
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K . Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. . Gene . 200 . 1–2 . 149–56 . 1997 . 9373149 . 10.1016/S0378-1119(97)00411-3 . etal.
• Strausberg RL, Feingold EA, Grouse LH . 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 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . etal. free .
• Strack B, Calistri A, Craig S . AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. . Cell . 114 . 6 . 689–99 . 2003 . 14505569 . 10.1016/S0092-8674(03)00653-6 . 10733770 . etal. free .
• von Schwedler UK, Stuchell M, Müller B . The protein network of HIV budding. . Cell . 114 . 6 . 701–13 . 2003 . 14505570 . 10.1016/S0092-8674(03)00714-1 . 16894972 . etal. free .
• Martin-Serrano J, Yarovoy A, Perez-Caballero D . 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 . 14519844 . 10.1073/pnas.2133846100 . 218772 . 2003PNAS..10012414M . etal. free .
• Peck JW, Bowden ET, Burbelo PD . Structure and function of human Vps20 and Snf7 proteins. . Biochem. J. . 377 . Pt 3 . 693–700 . 2004 . 14583093 . 10.1042/BJ20031347 . 1223912 .
• Ota T, Suzuki Y, Nishikawa T . Complete sequencing and characterization of 21,243 full-length human cDNAs. . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . etal. free .
• Gerhard DS, Wagner L, Feingold EA . The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . etal.
• Tsang HT, Connell JW, Brown SE . A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. . Genomics . 88 . 3 . 333–46 . 2006 . 16730941 . 10.1016/j.ygeno.2006.04.003 . etal. free .
• Ewing RM, Chu P, Elisma F . Large-scale mapping of human protein-protein interactions by mass spectrometry. . Mol. Syst. Biol. . 3 . 1. 89 . 2007 . 17353931 . 10.1038/msb4100134 . 1847948 . etal.

Notes and References

1. Howard TL, Stauffer DR, Degnin CR, Hollenberg SM . CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins . J Cell Sci . 114 . Pt 13 . 2395–404 . Sep 2001 . 10.1242/jcs.114.13.2395 . 11559748 .
2. Yorikawa C, Shibata H, Waguri S, Hatta K, Horii M, Katoh K, Kobayashi T, Uchiyama Y, Maki M . 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 . 15511219 . 1134928 . 10.1042/BJ20041227 .
3. Web site: CHMP6 charged multivesicular body protein 6 [Homo sapiens (human) ]].