Vif-mediated degradation of APOBEC3G

Li L, Li HS, Pauza CD, Bukrinsky M, Zhao RY. Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. Cell Res. 2005 Nov;15(11-12):923–34. doi: 10.1038/sj.cr.7290370. PMID: 16354571.; Kobayashi M, Takaori-Kondo A, Miyauchi Y, Iwai K, Uchiyama T. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C Complex Is Essential for Vif Function. Journal of Biological Chemistry. 2005 May;280(19):18573–8. doi: 10.1074/jbc.c500082200.; Yu X, Yu Y, Liu B, Luo K, Kong W, Mao P, Yu XF. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science. 2003 Nov 07;302(5647):1056–60. doi: 10.1126/science.1089591. PMID: 14564014.; Sheehy AM, Gaddis NC, Malim MH. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med. 2003 Nov;9(11):1404–7. doi: 10.1038/nm945. PMID: 14528300.; Stopak K, de Noronha C, Yonemoto W, Greene WC. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell. 2003 Sep;12(3):591–601. doi: 10.1016/s1097-2765(03)00353-8. PMID: 14527406.; Sheehy AM, Gaddis NC, Choi JD, Malim MH. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature. 2002 Aug 08;418(6898):646–50. doi: 10.1038/nature00939. PMID: 12167863.

Metabolites



Enzyme

EC Number name full name note
2.3.2.27 RING-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
2.3.2.32 cullin-RING-type E3 NEDD8 transferase [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine:[cullin] [NEDD8-protein] transferase (isopeptide bond-forming; RING-type)


Proteins

Protein ID name full name