The HIV-1 Vpr and glucocorticoid receptor complex is a gain-of-function interaction that prevents the nuclear localization of PARP-1

Nature Cell Biology

Volumn 8, Issue 2, 2006, Pages 170-179

  Muthumani, Karuppiah ^a   Choo, Andrew Y ^a,b   Zong, Wei Xing ^c   Madesh, Muniswamy ^c   Hwang, Daniel S ^a   Premkumar, Arumugam ^d   Thieu, Khanh P ^a   Emmanuel, Joann ^a   Kumar, Sanjeev ^a   Thompson, Craig B ^c   Weiner, David B ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; DEXAMETHASONE; GLUCOCORTICOID RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MIFEPRISTONE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; RECOMBINANT PROTEIN; SMALL INTERFERING RNA; VPR PROTEIN;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELLULAR DISTRIBUTION; COMPLEX FORMATION; CONTROLLED STUDY; DNA BINDING; GENE EXPRESSION REGULATION; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS INFECTION; IN VITRO STUDY; IN VIVO STUDY; MOUSE; NONHUMAN; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; RECEPTOR BINDING; TRANSCRIPTION REGULATION;

ACTIVE TRANSPORT, CELL NUCLEUS; ANIMALS; ANTIGENS, BACTERIAL; CELL LINE; CELL NUCLEUS; CERCOPITHECUS AETHIOPS; ENTEROTOXINS; FEMALE; GENE EXPRESSION; GENE PRODUCTS, VPR; HELA CELLS; HIV INFECTIONS; HUMANS; I-KAPPA B KINASE; I-KAPPA B PROTEINS; INTERLEUKIN-1; INTERLEUKIN-12; JURKAT CELLS; LIPOPOLYSACCHARIDES; MICE; MICE, INBRED BALB C; MIFEPRISTONE; MUTATION; NF-KAPPA B; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; RECEPTORS, GLUCOCORTICOID; RNA, SMALL INTERFERING; TRANSCRIPTION FACTOR RELA; TRANSFECTION; TUMOR NECROSIS FACTOR-ALPHA; U937 CELLS;

ANIMALIA; HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 33645147708     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1352     Document Type: Article

References (35)

1. Muthumani, K. et al. Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: Insights into the mechanism. Cell Death Differ. 12, 962-970 (2005).
2. Gandhi, R. T. & Walker, B. D. Immunologic control of HIV-1. Annu. Rev. Med. 53, 149-172 (2002).
3. Ho, D. D. et al. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection. Nature 373, 123-126 (1995).
4. Xu, X. N. et al. Evasion of cytotoxic T lymphocyte (CTL) responses by Nef-dependent induction of Fas ligand (CD95L) expression on simian immunodeficiency virus-infected cells. J. Exp. Med. 186, 7-16 (1997).
5. Letvin, N. L. Progress in the development of an HIV-1 vaccine. Science 280, 1875-1880 (1998).
6. Geleziunas, R. et al. HIV-1 Nef inhibits ASK1-dependent death signalling providing a potential mechanism for protecting the infected host cell. Nature 410, 834-838 (2001).
7. Muthumani, K. et al. Mechanism of HIV-1 viral protein R-induced apoptosis. Biochem. Biophys. Res. Commun. 304, 583-592 (2003).
8. Levy, D. N. et al. Serum Vpr regulates productive infection and latency of human immunodeficiency virus type 1. Proc. Natl Acad. Sci. USA 91, 10873-10877 (1994).
9. Levy, D. N., Refaeli, Y. & Weiner, D. B. Extracellular Vpr protein increases cellular permissiveness to human immunodeficiency virus replication and reactivates virus from latency. J. Virol. 69, 1243-1252 (1995).
10. Sherman, M. P. et al. HIV-1 vpr displays natural protein transducing properties: Implications for viral pathogenesis. Virology 302, 95-105 (2002).
11. Jowett, J. B. et al. Human immunodeficiency virus type 1 vpr gene arrests infected T cells in the G2 + M phase of the cell cycle. J. Virol. 69, 6304-6313 (1995).
12. Ayyavoo, V. et al. HIV-1 Vpr suppresses immune activation and apoptosis through regulation of nuclear factor κB. Nature Med. 3, 1117-1123 (1997).
13. Stewart, S. A. et al. Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest. J. Virol. 71, 5579-5592 (1997).
14. Goh, W. C. et al. HIV-1 Vpr increases viral expression by manipulation of the cell cycle: A mechanism for selection of Vpr in vivo. Nature Med. 4, 65-71 (1998).
15. Jacotot, E. et al. Control of mitochondrial membrane permeabilization by adenine nucleotide translocator interacting with HIV-1 viral protein R and Bcl-2. J. Exp. Med. 193, 509-519 (2001).
16. Muthumani, et al. HIV-1 Vpr induces apoptosis through caspase 9 in T cells and peripheral blood mononuclear cells. J. Biol. Chem. 277, 37820-37831 (2002).
17. Muthumani, K. et al. HIV-1 Vpr inhibits the maturation and activation of macrophages and dendritic cells in vitro. Int. Immunol. 17, 103-116 (2005).
18. de Noronha, C. M. et al. Dynamic disruptions in nuclear envelope architecture and integrity induced by HIV-1 Vpr. Science 294, 1105-1108 (2001).
19. Muthumani, K. et al. HIV-1 viral protein-R (Vpr) protects against lethal superantigen challenge while maintaining homeostatic T cell levels in vivo. Mol. Ther. 12, 910-921 (2005).
20. Refaeli, Y., Levy, D. N. & Weiner, D. B. The glucocorticoid receptor type II complex is a target of the HIV-1 vpr gene product. Proc. Natl Acad. Sci. USA 92, 3621-3625 (1995).
21. Kino, T. et al. The HIV-1 virion-associated protein vpr is a coactivator of the human glucocorticoid receptor. J. Exp. Med. 189, 51-62 (1999).
22. Ramanathan, M. P. et al. Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and glucocorticoid-mediated signaling. J. Biol. Chem. 277, 47854-47860 (2002).
23. Doppler, W. et al. Expression level-dependent contribution of glucocorticoid receptor domains for functional interaction with STAT5. Mol. Cell. Biol. 21, 3266-3279 (2001).
24. Chen, L. F. & Greene, W. C. Shaping the nuclear action of NF-kappaB. Nature Rev. Mol. Cell Biol. 5, 392-401 (2004).
25. Oliver, F.J. et al. Resistance to endotoxic shock as a consequence of defective NF-κB activation in poly(ADP-ribose) polymerase-1 deficient mice. EMBOJ. 18, 4446-4454 (1999).
26. Hassa, P. O. et al. The enzymatic and DNA binding activity of PARP-1 are not required for NF-κB coactivator function. J. Biol. Chem. 276, 45588-45597 (2001).
27. Chang, W. J. & Alvarez-Gonzalez, R. The sequence-specific DNA binding of NF-κB is reversibly regulated by the automodification reaction of poly (ADP-ribose) polymerase 1. J. Biol. Chem. 276, 47664-47670 (2001).
28. Hassa, P. O. et al. The enzymatic and DNA binding activity of PARP-1 are not required for NF-κB coactivator function. J. Biol. Chem. 276, 45588-45897 (2001).
29. Mahalingam, S. et al. Nuclear import, virion incorporation, and cell cycle arrest/differentiation are mediated by distinct functional domains of human immunodeficiency virus type 1 Vpr. J. Virol. 71, 6339-6347 (1997).
30. Arad, G. et al. Superantigen antagonist protects against lethal shock and defines a new domain for T-cell activation. Nature Med. 6, 414-421 (2000).
31. Kim, M. Y. et al. NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 119, 803-814 (2004).
32. Parent, M. et al. Poly(ADP-ribose) polymerase-1 is a negative regulator of HIV-1 transcription through competitive binding to TAR RNA with Tat-positive transcription elongation factor b (p-TEFb) complex. J. Biol. Chem. 280, 448-457 (2005).
33. Sawaya, B. E. et al. Cooperative interaction between HIV-1 regulatory proteins Tat and Vpr modulates transcription of the viral genome. J. Biol. Chem. 275, 35209-35214 (2000).
34. Kashanchi, F. et al. Cell cycle-regulated transcription by the human immunodeficiency virus type 1 Tat transactivator. J. Virol. 74, 652-660 (2000).
35. Zong, W.X. et al. Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev. 18, 1223-1226 (2004).