Polyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif

Journal of Virology

Volumn 84, Issue 9, 2010, Pages 4840-4844

  Shao, Qiujia ^a   Wang, Yudi ^a,b   Hildreth, James E K ^a   Liu, Bindong ^a  

^a MEHARRY MEDICAL COLLEGE   (United States)

^b JILIN UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; LYSINE; VIF PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; IN VIVO STUDY; MACACA; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STABILITY; SIMIAN IMMUNODEFICIENCY VIRUS; UBIQUITINATION;

CELL LINE; CYTIDINE DEAMINASE; HIV-1; HUMANS; SIMIAN IMMUNODEFICIENCY VIRUS; UBIQUITINATION; VIF GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS;

HUMAN IMMUNODEFICIENCY VIRUS 1; SIMIAN IMMUNODEFICIENCY VIRUS;

EID: 77950845533     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01911-09     Document Type: Article

References (30)

1. Akari, H., M. Fujita, S. Kao, M. A. Khan, M. Shehu-Xhilaga, A. Adachi, and K. Strebel. 2004. High level expression of human immunodeficiency virus type-1 Vif inhibits viral infectivity by modulating proteolytic processing of the Gag precursor at the p2/nucleocapsid processing site. J. Biol. Chem. 279:12355-12362.
2. Cadwell, K., and L. Coscoy. 2005. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 309:127-130.
3. Ciechanover, A., and R. Ben-Saadon. 2004. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 14:103-106. (Pubitemid 38293450)
4. Conticello, S. G., R. S. Harris, and M. S. Neuberger. 2003. The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G. Curr. Biol. 13:2009-2013.
5. Dang, Y., L. M. Siew, and Y. H. Zheng. 2008. APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated. J. Biol. Chem. 283:13124-13131.
6. Deshaies, R. J. 1999. SCF and Cullin/Ring H2-based ubiquitin ligases. Annu. Rev. Cell Dev. Biol. 15:435-467.
7. Fujita, M., H. Akari, A. Sakurai, A. Yoshida, T. Chiba, K. Tanaka, K. Strebel, and A. Adachi. 2004. Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation. Microbes Infect. 6:791-798. (Pubitemid 39055540)
8. Gaddis, N. C., A. M. Sheehy, K. M. Ahmad, C. M. Swanson, K. N. Bishop, B. E. Beer, P. A. Marx, F. Gao, F. Bibollet-Ruche, B. H. Hahn, and M. H. Malim. 2004. Further investigation of simian immunodeficiency virus Vif function in human cells. J. Virol. 78:12041-12046.
9. Galan, J. M., and M. Peter. 1999. Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism. Proc. Natl. Acad. Sci. U. S. A. 96:9124-9129.
10. Iwatani, Y., D. S. Chan, L. Liu, H. Yoshii, J. Shibata, N. Yamamoto, J. G. Levin, A. M. Gronenborn, and W. Sugiura. 2009. HIV-1 Vif-mediated ubiquitination/ degradation of APOBEC3G involves four critical lysine residues in its C-terminal domain. Proc. Natl. Acad. Sci. U. S. A. 106:19539-19544.
11. Izumi, T., A. Takaori-Kondo, K. Shirakawa, H. Higashitsuji, K. Itoh, K. Io, M. Matsui, K. Iwai, H. Kondoh, T. Sato, M. Tomonaga, S. Ikeda, H. Akari, Y. Koyanagi, J. Fujita, and T. Uchiyama. 2009. MDM2 is a novel E3 ligase for HIV-1 Vif. Retrovirology 6:1. doi:10.1186/1742-4690-6-1.
12. Kobayashi, M., A. Takaori-Kondo, Y. Miyauchi, K. Iwai, and T. Uchiyama. 2005. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. J. Biol. Chem. 280:18573-18578.
13. Li, Y., S. Gazdoiu, Z. Q. Pan, and S. Y. Fuchs. 2004. Stability of homologue of Slimb F-box protein is regulated by availability of its substrate. J. Biol. Chem. 279:11074-11080.
14. Liu, B., P. T. Sarkis, K. Luo, Y. Yu, and X. F. Yu. 2005. Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J. Virol. 79:9579-9587.
15. Luo, K., Z. Xiao, E. Ehrlich, Y. Yu, B. Liu, S. Zheng, and X. F. Yu. 2005. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc. Natl. Acad. Sci. U. S. A. 102:11444-11449.
16. Mariani, R., D. Chen, B. Schrofelbauer, F. Navarro, R. Konig, B. Bollman, C. Munk, H. Nymark-McMahon, and N. R. Landau. 2003. Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. Cell 114:21-31. (Pubitemid 36859838)
17. Marin, M., K. M. Rose, S. L. Kozak, and D. Kabat. 2003. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat. Med. 9:1398-1403.
18. Mehle, A., J. Goncalves, M. Santa-Marta, M. McPike, and D. Gabuzda. 2004. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev. 18: 2861-2866. (Pubitemid 39602304)
19. Mehle, A., B. Strack, P. Ancuta, C. Zhang, M. McPike, and D. Gabuzda. 2004. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 279:7792-7798.
20. Sheehy, A. M., N. C. Gaddis, J. D. Choi, and M. H. Malim. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650.
21. Sheehy, A. M., N. C. Gaddis, and M. H. Malim. 2003. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat. Med. 9:1404-1407.
22. Stanley, B. J., E. S. Ehrlich, L. Short, Y. Yu, Z. Xiao, X. F. Yu, and Y. Xiong. 2008. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J. Virol. 82:8656-8663.
23. Stopak, K., C. de Noronha, W. Yonemoto, and W. C. Greene. 2003. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol. Cell 12:591-601. (Pubitemid 37222482)
24. Wang, X., R. A. Herr, W. J. Chua, L. Lybarger, E. J. Wiertz, and T. H. Hansen. 2007. Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3. J. Cell Biol. 177:613-624. (Pubitemid 46799833)
25. Wirbelauer, C., H. Sutterluty, M. Blondel, M. Gstaiger, M. Peter, F. Reymond, and W. Krek. 2000. The F-box protein Skp2 is a ubiquitylation target of a Cul1-based core ubiquitin ligase complex: evidence for a role of Cul1 in the suppression of Skp2 expression in quiescent fibroblasts. EMBO J. 19: 5362-5375.
26. Yu, Q., D. Chen, R. Konig, R. Mariani, D. Unutmaz, and N. R. Landau. 2004. APOBEC3B and APOBEC3C are potent inhibitors of simian immunodeficiency virus replication. J. Biol. Chem. 279:53379-53386.
27. Yu, X., Y. Yu, B. Liu, K. Luo, W. Kong, P. Mao, and X. F. Yu. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060.
28. Yu, Y., Z. Xiao, E. S. Ehrlich, X. Yu, and X. F. Yu. 2004. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev. 18:2867-2872.
29. Zhang, W., M. Huang, T. Wang, L. Tan, C. Tian, X. Yu, W. Kong, and X. F. Yu. 2008. Conserved and non-conserved features of HIV-1 and SIVagm Vif mediated suppression of APOBEC3 cytidine deaminases. Cell. Microbiol. 10:1662-1675.
30. Zhou, P., and P. M. Howley. 1998. Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases. Mol. Cell 2:571-580. (Pubitemid 128379083)