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Volumn 374, Issue 1, 2007, Pages 121-129

Allosteric Loss-of-function Mutations in HIV-1 Nef from a Long-term Non-progressor

Author keywords

Hck; HIV 1; Nef; SH3 domain; Src family kinase

Indexed keywords

HEMATOPOIETIC CELL KINASE; NEF PROTEIN; PROTEIN SH3; PROTEIN TYROSINE KINASE;

EID: 35348957280     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.09.009     Document Type: Article
Times cited : (34)

References (40)
  • 1
    • 0036230879 scopus 로고    scopus 로고
    • Live and let die: Nef functions beyond HIV replication
    • Fackler O.T., and Baur A.S. Live and let die: Nef functions beyond HIV replication. Immunity 16 (2002) 493-497
    • (2002) Immunity , vol.16 , pp. 493-497
    • Fackler, O.T.1    Baur, A.S.2
  • 2
    • 0034565949 scopus 로고    scopus 로고
    • HIV-1 Nef: a critical factor in viral-induced pathogenesis
    • Greenway A.L., Holloway G., and McPhee D.A. HIV-1 Nef: a critical factor in viral-induced pathogenesis. Adv. Pharmacol. 48 (2000) 299-343
    • (2000) Adv. Pharmacol. , vol.48 , pp. 299-343
    • Greenway, A.L.1    Holloway, G.2    McPhee, D.A.3
  • 3
    • 4444273413 scopus 로고    scopus 로고
    • In vivo mutational analysis of the N-terminal region of HIV-1 Nef reveals critical motifs for the development of an AIDS-like disease in CD4C/HIV transgenic mice
    • Hanna Z., Priceputu E., Kay D.G., Poudrier J., Chrobak P., and Jolicoeur P. In vivo mutational analysis of the N-terminal region of HIV-1 Nef reveals critical motifs for the development of an AIDS-like disease in CD4C/HIV transgenic mice. Virology 327 (2004) 273-286
    • (2004) Virology , vol.327 , pp. 273-286
    • Hanna, Z.1    Priceputu, E.2    Kay, D.G.3    Poudrier, J.4    Chrobak, P.5    Jolicoeur, P.6
  • 4
    • 11444256754 scopus 로고    scopus 로고
    • Nef: "necessary and enforcing factor" in HIV infection
    • Joseph A.M., Kumar M., and Mitra D. Nef: "necessary and enforcing factor" in HIV infection. Curr. HIV Res. 3 (2005) 87-94
    • (2005) Curr. HIV Res. , vol.3 , pp. 87-94
    • Joseph, A.M.1    Kumar, M.2    Mitra, D.3
  • 7
    • 0028804160 scopus 로고
    • Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients
    • Deacon N.J., Tsykin A., Solomon A., Smith K., Ludford-Menting M., Hooker D.J., et al. Genomic structure of an attenuated quasi species of HIV-1 from a blood transfusion donor and recipients. Science 270 (1995) 988-991
    • (1995) Science , vol.270 , pp. 988-991
    • Deacon, N.J.1    Tsykin, A.2    Solomon, A.3    Smith, K.4    Ludford-Menting, M.5    Hooker, D.J.6
  • 8
    • 0029846223 scopus 로고    scopus 로고
    • High frequency of defective nef alleles in a long-term survivor with non-progressive human immunodeficiency virus type 1 infection
    • Mariani R., Kirchhoff F., Greenough T.C., Sullivan J.L., Desrosiers R.C., and Skowronski J. High frequency of defective nef alleles in a long-term survivor with non-progressive human immunodeficiency virus type 1 infection. J. Virol. 70 (1996) 7752-7764
    • (1996) J. Virol. , vol.70 , pp. 7752-7764
    • Mariani, R.1    Kirchhoff, F.2    Greenough, T.C.3    Sullivan, J.L.4    Desrosiers, R.C.5    Skowronski, J.6
  • 9
    • 0032538278 scopus 로고    scopus 로고
    • Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice
    • Hanna Z., Kay D.G., Rebai N., Guimond A., Jothy S., and Jolicoeur P. Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice. Cell 95 (1998) 163-175
    • (1998) Cell , vol.95 , pp. 163-175
    • Hanna, Z.1    Kay, D.G.2    Rebai, N.3    Guimond, A.4    Jothy, S.5    Jolicoeur, P.6
  • 10
    • 33645980955 scopus 로고    scopus 로고
    • Anti-CD45RO suppresses human immunodeficiency virus type 1 replication in microglia: role of Hck tyrosine kinase and implications for AIDS dementia
    • Kim M.O., Suh H.S., Si Q., Terman B.I., and Lee S.C. Anti-CD45RO suppresses human immunodeficiency virus type 1 replication in microglia: role of Hck tyrosine kinase and implications for AIDS dementia. J. Virol. 80 (2006) 62-72
    • (2006) J. Virol. , vol.80 , pp. 62-72
    • Kim, M.O.1    Suh, H.S.2    Si, Q.3    Terman, B.I.4    Lee, S.C.5
  • 11
    • 0041622820 scopus 로고    scopus 로고
    • CSF-induced and HIV-1-mediated distinct regulation of Hck and C/EBPbeta represent a heterogeneous susceptibility of monocyte-derived macrophages to M-tropic HIV-1 infection
    • Komuro I., Yokota Y., Yasuda S., Iwamoto A., and Kagawa K.S. CSF-induced and HIV-1-mediated distinct regulation of Hck and C/EBPbeta represent a heterogeneous susceptibility of monocyte-derived macrophages to M-tropic HIV-1 infection. J. Exp. Med. 198 (2003) 443-453
    • (2003) J. Exp. Med. , vol.198 , pp. 443-453
    • Komuro, I.1    Yokota, Y.2    Yasuda, S.3    Iwamoto, A.4    Kagawa, K.S.5
  • 12
    • 0034843329 scopus 로고    scopus 로고
    • The pathogenicity of human immunodeficiency virus (HIV) type 1 Nef in CD4C/HIV transgenic mice is abolished by mutation of its SH3-binding domain, and disease development is delayed in the absence of Hck
    • Hanna Z., Weng X., Kay D.G., Poudrier J., Lowell C., and Jolicoeur P. The pathogenicity of human immunodeficiency virus (HIV) type 1 Nef in CD4C/HIV transgenic mice is abolished by mutation of its SH3-binding domain, and disease development is delayed in the absence of Hck. J. Virol. 75 (2001) 9378-9392
    • (2001) J. Virol. , vol.75 , pp. 9378-9392
    • Hanna, Z.1    Weng, X.2    Kay, D.G.3    Poudrier, J.4    Lowell, C.5    Jolicoeur, P.6
  • 13
    • 0030792141 scopus 로고    scopus 로고
    • SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1
    • Briggs S.D., Sharkey M., Stevenson M., and Smithgall T.E. SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1. J. Biol. Chem. 272 (1997) 17899-17902
    • (1997) J. Biol. Chem. , vol.272 , pp. 17899-17902
    • Briggs, S.D.1    Sharkey, M.2    Stevenson, M.3    Smithgall, T.E.4
  • 14
    • 0036238473 scopus 로고    scopus 로고
    • SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo
    • Lerner E.C., and Smithgall T.E. SH3-dependent stimulation of Src-family kinase autophosphorylation without tail release from the SH2 domain in vivo. Nature Struct. Biol. 9 (2002) 365-369
    • (2002) Nature Struct. Biol. , vol.9 , pp. 365-369
    • Lerner, E.C.1    Smithgall, T.E.2
  • 15
    • 6344276677 scopus 로고    scopus 로고
    • Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase
    • Choi H.J., and Smithgall T.E. Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase. J. Mol. Biol. 343 (2004) 1255-1268
    • (2004) J. Mol. Biol. , vol.343 , pp. 1255-1268
    • Choi, H.J.1    Smithgall, T.E.2
  • 16
    • 33748751555 scopus 로고    scopus 로고
    • HIV-1 Nef selectively activates SRC family kinases HCK, LYN, and c-SRC through direct SH3 domain interaction
    • Trible R.P., Emert-Sedlak L., and Smithgall T.E. HIV-1 Nef selectively activates SRC family kinases HCK, LYN, and c-SRC through direct SH3 domain interaction. J. Biol. Chem. 281 (2006) 27029-27038
    • (2006) J. Biol. Chem. , vol.281 , pp. 27029-27038
    • Trible, R.P.1    Emert-Sedlak, L.2    Smithgall, T.E.3
  • 17
    • 0029881450 scopus 로고    scopus 로고
    • The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase
    • Grzesiek S., Bax A., Clore G.M., Gronenborn A.M., Hu J.S., Kaufman J., et al. The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase. Nature Struct. Biol. 3 (1996) 340-345
    • (1996) Nature Struct. Biol. , vol.3 , pp. 340-345
    • Grzesiek, S.1    Bax, A.2    Clore, G.M.3    Gronenborn, A.M.4    Hu, J.S.5    Kaufman, J.6
  • 18
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain
    • Lee C.H., Saksela K., Mirza U.A., Chait B.T., and Kuriyan J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85 (1996) 931-942
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 21
    • 0023377484 scopus 로고
    • Characterization of avian and viral p60src proteins expressed in yeast
    • Kornbluth S., Jove R., and Hanafusa H. Characterization of avian and viral p60src proteins expressed in yeast. Proc. Natl Acad. Sci. USA 84 (1987) 4455-4459
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4455-4459
    • Kornbluth, S.1    Jove, R.2    Hanafusa, H.3
  • 22
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., and Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol. Cell 3 (1999) 639-648
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 23
    • 0034723419 scopus 로고    scopus 로고
    • Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand
    • Porter M., Schindler T., Kuriyan J., and Miller W.T. Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand. J. Biol. Chem. 275 (2000) 2721-2726
    • (2000) J. Biol. Chem. , vol.275 , pp. 2721-2726
    • Porter, M.1    Schindler, T.2    Kuriyan, J.3    Miller, W.T.4
  • 24
    • 0028878783 scopus 로고
    • Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4
    • Saksela K., Cheng G., and Baltimore D. Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4. EMBO J. 14 (1995) 484-491
    • (1995) EMBO J. , vol.14 , pp. 484-491
    • Saksela, K.1    Cheng, G.2    Baltimore, D.3
  • 25
    • 0030696119 scopus 로고    scopus 로고
    • Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry
    • Engen J.R., Smithgall T.E., Gmeiner W.H., and Smith D.L. Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry. Biochemistry 36 (1997) 14384-14391
    • (1997) Biochemistry , vol.36 , pp. 14384-14391
    • Engen, J.R.1    Smithgall, T.E.2    Gmeiner, W.H.3    Smith, D.L.4
  • 27
    • 29344471038 scopus 로고    scopus 로고
    • An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry
    • Hochrein J.M., Lerner E.C., Schiavone A.P., Smithgall T.E., and Engen J.R. An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry. Protein Sci. 15 (2006) 65-73
    • (2006) Protein Sci. , vol.15 , pp. 65-73
    • Hochrein, J.M.1    Lerner, E.C.2    Schiavone, A.P.3    Smithgall, T.E.4    Engen, J.R.5
  • 28
    • 33645073892 scopus 로고    scopus 로고
    • Partial unfolding of diverse SH3 domains on a wide timescale
    • Wales T.E., and Engen J.R. Partial unfolding of diverse SH3 domains on a wide timescale. J. Mol. Biol. 357 (2006) 1592-1604
    • (2006) J. Mol. Biol. , vol.357 , pp. 1592-1604
    • Wales, T.E.1    Engen, J.R.2
  • 29
    • 33846576688 scopus 로고    scopus 로고
    • Characterization of intramolecular interactions of HIV-1 accessory protein Nef by differential scanning calorimetry
    • Groesch T.D., and Freire E. Characterization of intramolecular interactions of HIV-1 accessory protein Nef by differential scanning calorimetry. Biophys. Chem. 126 (2007) 36-42
    • (2007) Biophys. Chem. , vol.126 , pp. 36-42
    • Groesch, T.D.1    Freire, E.2
  • 30
    • 0033776709 scopus 로고    scopus 로고
    • HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes
    • Piguet V., Wan L., Borel C., Mangasarian A., Demaurex N., Thomas G., and Trono D. HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes. Nature Cell Biol. 2 (2000) 163-167
    • (2000) Nature Cell Biol. , vol.2 , pp. 163-167
    • Piguet, V.1    Wan, L.2    Borel, C.3    Mangasarian, A.4    Demaurex, N.5    Thomas, G.6    Trono, D.7
  • 31
    • 0037074008 scopus 로고    scopus 로고
    • HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway
    • Blagoveshchenskaya A.D., Thomas L., Feliciangeli S.F., Hung C.H., and Thomas G. HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell 111 (2002) 853-866
    • (2002) Cell , vol.111 , pp. 853-866
    • Blagoveshchenskaya, A.D.1    Thomas, L.2    Feliciangeli, S.F.3    Hung, C.H.4    Thomas, G.5
  • 32
    • 0035844009 scopus 로고    scopus 로고
    • Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef
    • Geyer M., and Peterlin B.M. Domain assembly, surface accessibility and sequence conservation in full length HIV-1 Nef. FEBS Letters 496 (2001) 91-95
    • (2001) FEBS Letters , vol.496 , pp. 91-95
    • Geyer, M.1    Peterlin, B.M.2
  • 34
    • 0035368515 scopus 로고    scopus 로고
    • Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein
    • Arold S.T., and Bauer A.S. Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein. Trends Biochem. Sci. 26 (2001) 356-363
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 356-363
    • Arold, S.T.1    Bauer, A.S.2
  • 35
    • 0141638487 scopus 로고    scopus 로고
    • Attenuated nef DNA vaccine construct induces cellular immune response: role in HIV-1 multiprotein vaccine
    • Majumder B., Gray B., McBurney S., Schaefer T.M., Dentchev T., Mahalingam S., et al. Attenuated nef DNA vaccine construct induces cellular immune response: role in HIV-1 multiprotein vaccine. Immunol. Letters 89 (2003) 207-214
    • (2003) Immunol. Letters , vol.89 , pp. 207-214
    • Majumder, B.1    Gray, B.2    McBurney, S.3    Schaefer, T.M.4    Dentchev, T.5    Mahalingam, S.6
  • 36
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • Kushnirov V.V. Rapid and reliable protein extraction from yeast. Yeast 16 (2000) 857-860
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 37
    • 33746882478 scopus 로고    scopus 로고
    • Conformational features of the full-length HIV and SIV Nef proteins determined by mass spectrometry
    • Hochrein J.M., Wales T.E., Lerner E.C., Schiavone A.P., Smithgall T.E., and Engen J.R. Conformational features of the full-length HIV and SIV Nef proteins determined by mass spectrometry. Biochemistry 45 (2006) 7733-7739
    • (2006) Biochemistry , vol.45 , pp. 7733-7739
    • Hochrein, J.M.1    Wales, T.E.2    Lerner, E.C.3    Schiavone, A.P.4    Smithgall, T.E.5    Engen, J.R.6
  • 38
    • 0028805516 scopus 로고
    • A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein
    • Lee C.H., Leung B., Lemmon M.A., Zheng J., Cowburn D., Kuriyan J., and Saksela K. A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein. EMBO J. 14 (1995) 5006-5015
    • (1995) EMBO J. , vol.14 , pp. 5006-5015
    • Lee, C.H.1    Leung, B.2    Lemmon, M.A.3    Zheng, J.4    Cowburn, D.5    Kuriyan, J.6    Saksela, K.7
  • 39
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation
    • Zhang Z., and Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci. 2 (1993) 522-531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 40
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales T.E., and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25 (2006) 158-170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2


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