메뉴 건너뛰기




Volumn 505, Issue 7482, 2014, Pages 234-238

Structural basis of lentiviral subversion of a cellular protein degradation pathway

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CELL PROTEIN; LIGASE; PROTEIN DCAF1; PROTEIN SAMHD1; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRAL ACCESSORY PROTEIN X; VIRUS PROTEIN;

EID: 84892171421     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12815     Document Type: Article
Times cited : (107)

References (25)
  • 1
    • 79959843617 scopus 로고    scopus 로고
    • SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx
    • Laguette, N. et al. SAMHD1 is the dendritic-and myeloid-cell-specific HIV-1 restriction factor counteracted by Vpx. Nature 474, 654-657 (2011).
    • (2011) Nature , vol.474 , pp. 654-657
    • Laguette, N.1
  • 2
    • 79959858243 scopus 로고    scopus 로고
    • Vpx relieves inhibition of HIV-1 infection ofmacrophagesmediated by the SAMHD1 protein
    • Hrecka, K. et al.Vpx relieves inhibition of HIV-1 infection ofmacrophagesmediated by the SAMHD1 protein. Nature 474, 658-661 (2011).
    • (2011) Nature , vol.474 , pp. 658-661
    • Hrecka, K.1
  • 3
    • 84869170593 scopus 로고    scopus 로고
    • SAMHD1 restricts HIV-1 infection in resting CD41 T cells
    • Baldauf, H. M. et al. SAMHD1 restricts HIV-1 infection in resting CD41 T cells. Nature Med. 18, 1682-1689 (2012).
    • (2012) Nature Med. , vol.18 , pp. 1682-1689
    • Baldauf, H.M.1
  • 4
    • 84867672682 scopus 로고    scopus 로고
    • SAMHD1restricts HIV-1 reverse transcription inquiescentCD41 T-cells
    • Descours, B. et al. SAMHD1restricts HIV-1 reverse transcription inquiescentCD41 T-cells. Retrovirology 9, 87 (2012).
    • (2012) Retrovirology , vol.9 , pp. 87
    • Descours, B.1
  • 5
    • 83555164881 scopus 로고    scopus 로고
    • HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase
    • Goldstone, D. C. et al. HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase. Nature 480, 379-382 (2011).
    • (2011) Nature , vol.480 , pp. 379-382
    • Goldstone, D.C.1
  • 6
    • 84862777555 scopus 로고    scopus 로고
    • SAMHD1 restricts the replication of humanimmunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates
    • Lahouassa, H. et al. SAMHD1 restricts the replication of humanimmunodeficiency virus type 1 by depleting the intracellular pool of deoxynucleoside triphosphates. Nature Immunol. 13, 223-228 (2012).
    • (2012) Nature Immunol , vol.13 , pp. 223-228
    • Lahouassa, H.1
  • 7
    • 84857347109 scopus 로고    scopus 로고
    • The ability of primate lentiviruses to degrade the monocyte restriction factor SAMHD1 preceded the birth of the viral accessory protein Vpx
    • Lim, E. S. et al. The ability of primate lentiviruses to degrade the monocyte restriction factor SAMHD1 preceded the birth of the viral accessory protein Vpx. Cell Host Microbe 11, 194-204 (2012).
    • (2012) Cell Host Microbe , vol.11 , pp. 194-204
    • Lim, E.S.1
  • 8
    • 84859482628 scopus 로고    scopus 로고
    • HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1
    • Ahn, J. et al. HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1. J. Biol. Chem. 287, 12550-12558 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 12550-12558
    • Ahn, J.1
  • 10
    • 84867629398 scopus 로고    scopus 로고
    • A novel DCAF1-bindingmotif required for Vpx-mediated degradation of nuclear SAMHD1 and Vpr-induced G2 arrest
    • Wei, W. et al. A novel DCAF1-bindingmotif required for Vpx-mediated degradation of nuclear SAMHD1 and Vpr-induced G2 arrest. Cell. Microbiol. 14, 1745-1756 (2012).
    • (2012) Cell. Microbiol , vol.14 , pp. 1745-1756
    • Wei, W.1
  • 11
    • 44449107162 scopus 로고    scopus 로고
    • Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection
    • Srivastava, S. et al. Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection. PLoS Pathog. 4, e1000059 (2008).
    • (2008) PLoS Pathog. , vol.4
    • Srivastava, S.1
  • 12
    • 65349104493 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 2 Vpx protein usurps theCUL4A-DDB1DCAF1ubiquitin ligase to overcomea postentry block in macrophage infection
    • Bergamaschi, A. et al. The human immunodeficiency virus type 2 Vpx protein usurps theCUL4A-DDB1DCAF1ubiquitin ligase to overcomea postentry block in macrophage infection. J. Virol. 83, 4854-4860 (2009).
    • (2009) J. Virol. , vol.83 , pp. 4854-4860
    • Bergamaschi, A.1
  • 13
    • 84879579348 scopus 로고    scopus 로고
    • HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasomedependent degradation
    • DeLucia, M., Mehrens, J., Wu, Y. & Ahn, J. HIV-2 and SIVmac accessory virulence factor Vpx down-regulates SAMHD1 enzyme catalysis prior to proteasomedependent degradation. J. Biol. Chem. 288, 19116-19126 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 19116-19126
    • Delucia, M.1    Mehrens, J.2    Wu, Y.3    Ahn, J.4
  • 14
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett, E. J., Bence, N. F., Jayakumar, R. & Kopito, R. R. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol. Cell 17, 351-365 (2005).
    • (2005) Mol. Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 15
    • 57749198023 scopus 로고    scopus 로고
    • Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex
    • Scrima, A. et al. Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell 135, 1213-1223 (2008).
    • (2008) Cell , vol.135 , pp. 1213-1223
    • Scrima, A.1
  • 16
    • 81855227619 scopus 로고    scopus 로고
    • The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation
    • Fischer, E. S. et al. The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation. Cell 147, 1024-1039 (2011).
    • (2011) Cell , vol.147 , pp. 1024-1039
    • Fischer, E.S.1
  • 17
    • 84876240156 scopus 로고    scopus 로고
    • Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection
    • Yan, J. et al. Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection. J. Biol. Chem. 288, 10406-10417 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 10406-10417
    • Yan, J.1
  • 18
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • Angers, S. et al. Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443, 590-593 (2006).
    • (2006) Nature , vol.443 , pp. 590-593
    • Angers, S.1
  • 19
    • 77449113802 scopus 로고    scopus 로고
    • A promiscuous a-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery
    • Li, T., Robert, E. I., van Breugel, P. C., Strubin, M. & Zheng, N. A promiscuous a-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery. Nature Struct. Mol. Biol. 17, 105-111 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 105-111
    • Li, T.1    Robert, E.I.2    Van Breugel, P.C.3    Strubin, M.4    Zheng, N.5
  • 20
    • 84884745681 scopus 로고    scopus 로고
    • Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1
    • Fregoso, O. I. et al. Evolutionary toggling of Vpx/Vpr specificity results in divergent recognition of the restriction factor SAMHD1. PLoS Pathog. 9, e1003496 (2013).
    • (2013) PLoS Pathog , vol.9
    • Fregoso, O.I.1
  • 21
    • 34848911347 scopus 로고    scopus 로고
    • The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A-containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor
    • Wen, X., Duus, K. M., Friedrich, T. D. & de Noronha, C. M. The HIV1 protein Vpr acts to promote G2 cell cycle arrest by engaging a DDB1 and Cullin4A-containing ubiquitin ligase complex using VprBP/DCAF1 as an adaptor. J. Biol. Chem. 282, 27046-27057 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 27046-27057
    • Wen, X.1    Duus, K.M.2    Friedrich, T.D.3    De Noronha, C.M.4
  • 22
    • 34247187942 scopus 로고    scopus 로고
    • HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1
    • Schrö felbauer, B., Hakata, Y. & Landau, N. R. HIV-1 Vpr function is mediated by interaction with the damage-specific DNA-binding protein DDB1. Proc. Natl Acad. Sci. USA 104, 4130-4135 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 4130-4135
    • Schrö Felbauer, B.1
  • 23
    • 33846899500 scopus 로고    scopus 로고
    • HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase
    • Le Rouzic, E. et al. HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase. Cell Cycle 6, 182-188 (2007).
    • (2007) Cell Cycle , vol.6 , pp. 182-188
    • Le Rouzic, E.1
  • 24
    • 34547395804 scopus 로고    scopus 로고
    • Lentiviral Vpr usurps Cul4-DDB1[VprBP] E3 ubiquitin ligase to modulate cell cycle
    • Hrecka, K. et al. Lentiviral Vpr usurps Cul4-DDB1[VprBP] E3 ubiquitin ligase to modulate cell cycle. Proc. Natl Acad. Sci. USA 104, 11778-11783 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11778-11783
    • Hrecka, K.1
  • 25
    • 80052827178 scopus 로고    scopus 로고
    • Exposed hydrophobic residues in human immunodeficiency virus type 1 Vpr helix-1 are important for cell cycle arrest and cell death
    • Barnitz, R. A., Chaigne-Delalande, B., Bolton, D. L. & Lenardo, M. J. Exposed hydrophobic residues in human immunodeficiency virus type 1 Vpr helix-1 are important for cell cycle arrest and cell death. PLoS ONE 6, e24924 (2011).
    • (2011) PLoS ONE , vol.6
    • Barnitz, R.A.1    Chaigne-Delalande, B.2    Bolton, D.L.3    Lenardo, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.