The protein encoded by this gene is one of the eight subunits of COP9 signalosome, a highly conserved protein complex that functions as an important regulator in multiple signaling pathways. The structure and function of COP9 signalosome is similar to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome has been shown to interact with SCF-type E3 ubiquitin ligases and act as a positive regulator of E3 ubiquitin ligases. This protein belongs to translation initiation factor 3 (eIF3) superfamily. It is involved in the regulation of cell cycle and likely to be a cellular cofactor for HIV-1 accessory gene product Vpr.[2]
↑Hoareau Alves K, Bochard V, Réty S, Jalinot P (Sep 2002). "Association of the mammalian proto-oncoprotein Int-6 with the three protein complexes eIF3, COP9 signalosome and 26S proteasome". FEBS Lett. 527 (1–3): 15–21. doi:10.1016/S0014-5793(02)03147-2. PMID12220626.
Further reading
Wolf DA, Zhou C, Wee S (2004). "The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?". Nat. Cell Biol. 5 (12): 1029–33. doi:10.1038/ncb1203-1029. PMID14647295.
Muthumani K, Choo AY, Premkumar A, Hwang DS, Thieu KP, Desai BM, Weiner DB (2006). "Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism". Cell Death Differ. 12 Suppl 1: 962–70. doi:10.1038/sj.cdd.4401583. PMID15832179.
Mittmeyer HJ (1976). "[Distribution pattern of rigor mortis in various joint regions]". Beitr. Gerichtl. Med. 33: 85–96. PMID1222062.
Zhao LJ, Mukherjee S, Narayan O (1994). "Biochemical mechanism of HIV-I Vpr function. Specific interaction with a cellular protein". J. Biol. Chem. 269 (22): 15577–82. PMID8195203.
Seeger M, Kraft R, Ferrell K, Bech-Otschir D, Dumdey R, Schade R, Gordon C, Naumann M, Dubiel W (1998). "A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits". FASEB J. 12 (6): 469–78. PMID9535219.
Wei N, Tsuge T, Serino G, Dohmae N, Takio K, Matsui M, Deng XW (1998). "The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex". Curr. Biol. 8 (16): 919–22. doi:10.1016/S0960-9822(07)00372-7. PMID9707402.
Elder RT, Yu M, Chen M, Edelson S, Zhao Y (2000). "Cell cycle G2 arrest induced by HIV-1 Vpr in fission yeast (Schizosaccharomyces pombe) is independent of cell death and early genes in the DNA damage checkpoint". Virus Res. 68 (2): 161–73. doi:10.1016/S0168-1702(00)00167-2. PMID10958988.
Ramanathan MP, Ayyavoo V, Weiner DB (2001). "Choice of expression vector alters the localization of a human cellular protein". DNA Cell Biol. 20 (2): 101–5. doi:10.1089/104454901750070300. PMID11244567.
Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, Zhou C, Wolf DA, Wei N, Shevchenko A, Deshaies RJ (2001). "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome". Science. 292 (5520): 1382–5. doi:10.1126/science.1059780. PMID11337588.
Elder RT, Yu M, Chen M, Zhu X, Yanagida M, Zhao Y (2001). "HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25". Virology. 287 (2): 359–70. doi:10.1006/viro.2001.1007. PMID11531413.