The HIV-1 Vpr and glucocorticoid receptor complex is a gain-of-function interaction that prevents the nuclear localization of PARP-1
10.1038/ncb1352
Crossref journal-article
Springer Science and Business Media LLC
Nature Cell Biology (297)
Bibliography

Muthumani, K., Choo, A. Y., Zong, W.-X., Madesh, M., Hwang, D. S., Premkumar, A., Thieu, K. P., Emmanuel, J., Kumar, S., Thompson, C. B., & Weiner, D. B. (2006). 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, 8(2), 170–179.

Authors 11
  1. Karuppiah Muthumani (first)
  2. Andrew Y. Choo (additional)
  3. Wei-Xing Zong (additional)
  4. Muniswamy Madesh (additional)
  5. Daniel S. Hwang (additional)
  6. Arumugam Premkumar (additional)
  7. Khanh P. Thieu (additional)
  8. Joann Emmanuel (additional)
  9. Sanjeev Kumar (additional)
  10. Craig B. Thompson (additional)
  11. David B. Weiner (additional)
References 35 Referenced 62
  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). (10.1038/sj.cdd.4401583) / Cell Death Differ. by K Muthumani (2005)
  2. Gandhi, R. T. & Walker, B. D. Immunologic control of HIV-1. Annu. Rev. Med. 53, 149–172 (2002). (10.1146/annurev.med.53.082901.104011) / Annu. Rev. Med. by RT Gandhi (2002)
  3. Ho, D. D. et al. Rapid turnover of plasma virions and CD4 lymphocytes in HIV-1 infection. Nature 373, 123–126 (1995). (10.1038/373123a0) / Nature by DD Ho (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). (10.1084/jem.186.1.7) / J. Exp. Med by XN Xu (1997)
  5. Letvin, N. L. Progress in the development of an HIV-1 vaccine. Science 280, 1875–1880 (1998). (10.1126/science.280.5371.1875) / Science by NL Letvin (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). (10.1038/35071111) / Nature by R Geleziunas (2001)
  7. Muthumani, K. et al. Mechanism of HIV-1 viral protein R-induced apoptosis. Biochem. Biophys. Res. Commun. 304, 583–592 (2003). (10.1016/S0006-291X(03)00631-4) / Biochem. Biophys. Res. Commun. by K Muthumani (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). (10.1073/pnas.91.23.10873) / Proc. Natl Acad. Sci. USA by DN Levy (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). (10.1128/jvi.69.2.1243-1252.1995) / J. Virol. by DN Levy (1995)
  10. Sherman, M. P. et al. HIV-1 vpr displays natural protein transducing properties: implications for viral pathogenesis. Virology 302, 95–105 (2002). (10.1006/viro.2002.1576) / Virology by MP Sherman (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). (10.1128/jvi.69.10.6304-6313.1995) / J. Virol. by JB Jowett (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). (10.1038/nm1097-1117) / Nature Med. by V Ayyavoo (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). (10.1128/jvi.71.7.5579-5592.1997) / J. Virol. by SA Stewart (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). (10.1038/nm0198-065) / Nature Med. by WC Goh (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). (10.1084/jem.193.4.509) / J. Exp. Med. by E Jacotot (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). (10.1074/jbc.M205313200) / J. Biol. Chem. by Muthumani (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). (10.1093/intimm/dxh190) / Int. Immunol. by K Muthumani (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). (10.1126/science.1063957) / Science by CM de Noronha (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). (10.1016/j.ymthe.2005.05.009) / Mol. Ther. by K Muthumani (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). (10.1073/pnas.92.8.3621) / Proc. Natl Acad. Sci. USA by Y Refaeli (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). (10.1084/jem.189.1.51) / J. Exp. Med. by T Kino (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). (10.1074/jbc.M203905200) / J. Biol. Chem. by MP Ramanathan (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). (10.1128/MCB.21.9.3266-3279.2001) / Mol. Cell. Biol. by W Doppler (2001)
  24. Chen, L. F. & Greene, W. C. Shaping the nuclear action of NF-kappaB. Nature Rev. Mol. Cell Biol. 5, 392–401 (2004). (10.1038/nrm1368) / Nature Rev. Mol. Cell Biol by LF Chen (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. EMBO J. 18, 4446–4454 (1999). (10.1093/emboj/18.16.4446) / EMBO J. by FJ Oliver (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). (10.1074/jbc.M106528200) / J. Biol. Chem. by PO Hassa (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). (10.1074/jbc.M104666200) / J. Biol. Chem. by WJ Chang (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). (10.1074/jbc.M106528200) / J. Biol. Chem. by PO Hassa (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). (10.1128/jvi.71.9.6339-6347.1997) / J. Virol. by S Mahalingam (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). (10.1038/74672) / Nature Med by G Arad (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). (10.1016/j.cell.2004.11.002) / Cell by MY Kim (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). (10.1074/jbc.M408435200) / J. Biol. Chem by M Parent (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). (10.1074/jbc.M005197200) / J. Biol. Chem. by BE Sawaya (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). (10.1128/JVI.74.2.652-660.2000) / J. Virol. by F Kashanchi (2000)
  35. Zong, W.X. et al. Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev. 18, 1223–1226 (2004). (10.1101/gad.1212404) / Genes Dev by WX Zong (2004)
Dates
Type When
Created 19 years, 7 months ago (Jan. 22, 2006, 1:25 p.m.)
Deposited 3 years, 5 months ago (March 25, 2022, 10 a.m.)
Indexed 5 months ago (March 30, 2025, 1:04 a.m.)
Issued 19 years, 7 months ago (Jan. 22, 2006)
Published 19 years, 7 months ago (Jan. 22, 2006)
Published Online 19 years, 7 months ago (Jan. 22, 2006)
Published Print 19 years, 6 months ago (Feb. 1, 2006)
Funders 0

None

@article{Muthumani_2006, title={The HIV-1 Vpr and glucocorticoid receptor complex is a gain-of-function interaction that prevents the nuclear localization of PARP-1}, volume={8}, ISSN={1476-4679}, url={http://dx.doi.org/10.1038/ncb1352}, DOI={10.1038/ncb1352}, number={2}, journal={Nature Cell Biology}, publisher={Springer Science and Business Media LLC}, author={Muthumani, Karuppiah and Choo, Andrew Y. and Zong, Wei-Xing and Madesh, Muniswamy and Hwang, Daniel S. and Premkumar, Arumugam and Thieu, Khanh P. and Emmanuel, Joann and Kumar, Sanjeev and Thompson, Craig B. and Weiner, David B.}, year={2006}, month=jan, pages={170–179} }