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Volumn 346, Issue 1, 2006, Pages 194-204

HTLV-1 Gag protein associates with CD82 tetraspanin microdomains at the plasma membrane

Author keywords

CD82; HIV 1; HTLV 1; Immune synapse; Retrovirus; T cells; Tetraspanins

Indexed keywords

CD82 ANTIGEN; CELL EXTRACT; GAG PROTEIN; MATRIX PROTEIN; TETRASPANIN;

EID: 32844458333     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2005.10.033     Document Type: Article
Times cited : (40)

References (46)
  • 1
    • 0347382581 scopus 로고    scopus 로고
    • The immune control and cell-to-cell spread of human T-lymphotropic virus type 1
    • C.R. Bangham The immune control and cell-to-cell spread of human T-lymphotropic virus type 1 J. Gen. Virol. 84 Pt. 12 2003 3177 3189
    • (2003) J. Gen. Virol. , vol.84 , Issue.12 PART , pp. 3177-3189
    • Bangham, C.R.1
  • 2
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • F. Berditchevski Complexes of tetraspanins with integrins: more than meets the eye J. Cell Sci. 114 Pt. 23 2001 4143 4151
    • (2001) J. Cell Sci. , vol.114 , Issue.23 PART , pp. 4143-4151
    • Berditchevski, F.1
  • 3
    • 0035162539 scopus 로고    scopus 로고
    • KAI1, a prostate metastasis suppressor: Prediction of solvated structure and interactions with binding partners; Integrins, cadherins, and cell-surface receptor proteins
    • R.J. Bienstock, and J.C. Barrett KAI1, a prostate metastasis suppressor: prediction of solvated structure and interactions with binding partners; integrins, cadherins, and cell-surface receptor proteins Mol. Carcinog. 32 3 2001 139 153
    • (2001) Mol. Carcinog. , vol.32 , Issue.3 , pp. 139-153
    • Bienstock, R.J.1    Barrett, J.C.2
  • 4
    • 0037783536 scopus 로고    scopus 로고
    • Role of myristylation in HIV-1 Gag assembly
    • F. Bouamr, S. Scarlata, and C. Carter Role of myristylation in HIV-1 Gag assembly Biochemistry 42 21 2003 6408 6417
    • (2003) Biochemistry , vol.42 , Issue.21 , pp. 6408-6417
    • Bouamr, F.1    Scarlata, S.2    Carter, C.3
  • 7
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts
    • C. Claas, C.S. Stipp, and M.E. Hemler Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts J. Biol. Chem. 276 11 2001 7974 7984
    • (2001) J. Biol. Chem. , vol.276 , Issue.11 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 8
    • 0346734190 scopus 로고    scopus 로고
    • Superantigen stimulation reveals the contribution of Lck to negative regulation of T cell activation
    • G. Criado, and J. Madrenas Superantigen stimulation reveals the contribution of Lck to negative regulation of T cell activation J. Immunol. 172 1 2004 222 230
    • (2004) J. Immunol. , vol.172 , Issue.1 , pp. 222-230
    • Criado, G.1    Madrenas, J.2
  • 9
    • 0037079628 scopus 로고    scopus 로고
    • Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes
    • A. Delaguillaumie, C. Lagaudriere-Gesbert, M.R. Popoff, and H. Conjeaud Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes J. Cell Sci. 115 Pt. 2 2002 433 443
    • (2002) J. Cell Sci. , vol.115 , Issue.2 PART , pp. 433-443
    • Delaguillaumie, A.1    Lagaudriere-Gesbert, C.2    Popoff, M.R.3    Conjeaud, H.4
  • 10
    • 9444291849 scopus 로고    scopus 로고
    • Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: Relevance to co-stimulation
    • A. Delaguillaumie, J. Harriague, S. Kohanna, G. Bismuth, E. Rubinstein, M. Seigneuret, and H. Conjeaud Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: relevance to co-stimulation J. Cell Sci. 117 Pt. 22 2004 5269 5282
    • (2004) J. Cell Sci. , vol.117 , Issue.22 PART , pp. 5269-5282
    • Delaguillaumie, A.1    Harriague, J.2    Kohanna, S.3    Bismuth, G.4    Rubinstein, E.5    Seigneuret, M.6    Conjeaud, H.7
  • 11
    • 0037436465 scopus 로고    scopus 로고
    • Virology. Forced entry-Or does HTLV-I have the key?
    • D. Derse, and G. Heidecker Virology. Forced entry-Or does HTLV-I have the key? Science 299 5613 2003 1670 1671
    • (2003) Science , vol.299 , Issue.5613 , pp. 1670-1671
    • Derse, D.1    Heidecker, G.2
  • 12
    • 0029880544 scopus 로고    scopus 로고
    • Examining the molecular genetics of HTLV-I with an infectious molecular clone of the virus and permissive cell culture systems
    • D. Derse, J. Mikovits, D. Waters, S. Brining, and F. Ruscetti Examining the molecular genetics of HTLV-I with an infectious molecular clone of the virus and permissive cell culture systems J. Acquired Immune Defic. Syndr. Hum. Retrovirol. 12 1996 1 5
    • (1996) J. Acquired Immune Defic. Syndr. Hum. Retrovirol. , vol.12 , pp. 1-5
    • Derse, D.1    Mikovits, J.2    Waters, D.3    Brining, S.4    Ruscetti, F.5
  • 13
    • 0034887093 scopus 로고    scopus 로고
    • Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors
    • D. Derse, S.A. Hill, P.A. Lloyd, H. Chung, and B.A. Morse Examining human T-lymphotropic virus type 1 infection and replication by cell-free infection with recombinant virus vectors J. Virol. 75 18 2001 8461 8468
    • (2001) J. Virol. , vol.75 , Issue.18 , pp. 8461-8468
    • Derse, D.1    Hill, S.A.2    Lloyd, P.A.3    Chung, H.4    Morse, B.A.5
  • 14
    • 0026600904 scopus 로고
    • Infection of peripheral blood mononuclear cells and cell lines by cell-free human T-cell lymphoma/leukemia virus type I
    • N. Fan, J. Gavalchin, B. Paul, K.H. Wells, M.J. Lane, and B.J. Poiesz Infection of peripheral blood mononuclear cells and cell lines by cell-free human T-cell lymphoma/leukemia virus type I J. Clin. Microbiol. 30 4 1992 905 910
    • (1992) J. Clin. Microbiol. , vol.30 , Issue.4 , pp. 905-910
    • Fan, N.1    Gavalchin, J.2    Paul, B.3    Wells, K.H.4    Lane, M.J.5    Poiesz, B.J.6
  • 15
    • 2642552933 scopus 로고    scopus 로고
    • Late assembly motifs of human T-cell leukemia virus type 1 and their relative roles in particle release
    • G. Heidecker, K. Fox, K. Nagashima, and D. Derse Late assembly motifs of human T-cell leukemia virus type 1 and their relative roles in particle release J. Virol. 78 2004 6636 6648
    • (2004) J. Virol. , vol.78 , pp. 6636-6648
    • Heidecker, G.1    Fox, K.2    Nagashima, K.3    Derse, D.4
  • 16
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • M.E. Hemler Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain Annu. Rev. Cell Dev. Biol. 19 2003 397 422
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 17
    • 0037384986 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly and lipid rafts: Pr55 (gag) associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100
    • K. Holm, K. Weclewicz, R. Hewson, and M. Suomalainen Human immunodeficiency virus type 1 assembly and lipid rafts: Pr55 (gag) associates with membrane domains that are largely resistant to Brij98 but sensitive to Triton X-100 J. Virol. 77 8 2003 4805 4817
    • (2003) J. Virol. , vol.77 , Issue.8 , pp. 4805-4817
    • Holm, K.1    Weclewicz, K.2    Hewson, R.3    Suomalainen, M.4
  • 19
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • P.S. Kabouridis, J. Janzen, A.L. Magee, and S.C. Ley Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes Eur. J. Immunol. 30 3 2000 954 963
    • (2000) Eur. J. Immunol. , vol.30 , Issue.3 , pp. 954-963
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 21
    • 0031569284 scopus 로고    scopus 로고
    • The tetraspanin protein CD82 associates with both free HLA class I heavy chain and heterodimeric beta 2-microglobulin complexes
    • C. Lagaudriere-Gesbert, S. Lebel-Binay, E. Wiertz, H.L. Ploegh, D. Fradelizi, and H. Conjeaud The tetraspanin protein CD82 associates with both free HLA class I heavy chain and heterodimeric beta 2-microglobulin complexes J. Immunol. 158 6 1997 2790 2797
    • (1997) J. Immunol. , vol.158 , Issue.6 , pp. 2790-2797
    • Lagaudriere-Gesbert, C.1    Lebel-Binay, S.2    Wiertz, E.3    Ploegh, H.L.4    Fradelizi, D.5    Conjeaud, H.6
  • 22
    • 0033019287 scopus 로고    scopus 로고
    • Multiple functions for the basic amino acids of the human T-cell leukemia virus type 1 matrix protein in viral transmission
    • I. Le Blanc, A.R. Rosenberg, and M.C. Dokhelar Multiple functions for the basic amino acids of the human T-cell leukemia virus type 1 matrix protein in viral transmission J. Virol. 73 3 1999 1860 1867
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 1860-1867
    • Le Blanc, I.1    Rosenberg, A.R.2    Dokhelar, M.C.3
  • 23
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • S. Levy, and T. Shoham The tetraspanin web modulates immune-signalling complexes Nat. Rev., Immunol. 5 2 2005 136 148
    • (2005) Nat. Rev., Immunol. , vol.5 , Issue.2 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 24
    • 0037114132 scopus 로고    scopus 로고
    • Cutting edge: Dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC
    • M. Mittelbrunn, M. Yanez-Mo, D. Sancho, A. Ursa, and F. Sanchez-Madrid Cutting edge: dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC J. Immunol. 169 12 2002 6691 6695
    • (2002) J. Immunol. , vol.169 , Issue.12 , pp. 6691-6695
    • Mittelbrunn, M.1    Yanez-Mo, M.2    Sancho, D.3    Ursa, A.4    Sanchez-Madrid, F.5
  • 25
    • 0035889958 scopus 로고    scopus 로고
    • Superantigen-induced T cell:B cell conjugation is mediated by LFA-1 and requires signaling through Lck, but not ZAP-70
    • M.M. Morgan, C.M. Labno, G.A. Van Seventer, M.F. Denny, D.B. Straus, and J.K. Burkhardt Superantigen-induced T cell:B cell conjugation is mediated by LFA-1 and requires signaling through Lck, but not ZAP-70 J. Immunol. 167 10 2001 5708 5718
    • (2001) J. Immunol. , vol.167 , Issue.10 , pp. 5708-5718
    • Morgan, M.M.1    Labno, C.M.2    Van Seventer, G.A.3    Denny, M.F.4    Straus, D.B.5    Burkhardt, J.K.6
  • 26
    • 4544232723 scopus 로고    scopus 로고
    • Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative
    • B. Muller, J. Daecke, O.T. Fackler, M.T. Dittmar, H. Zentgraf, and H.G. Krausslich Construction and characterization of a fluorescently labeled infectious human immunodeficiency virus type 1 derivative J. Virol. 78 2004 10803 10813
    • (2004) J. Virol. , vol.78 , pp. 10803-10813
    • Muller, B.1    Daecke, J.2    Fackler, O.T.3    Dittmar, M.T.4    Zentgraf, H.5    Krausslich, H.G.6
  • 27
  • 28
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • D.H. Nguyen, and J.E. Hildreth Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts J. Virol. 74 7 2000 3264 3272
    • (2000) J. Virol. , vol.74 , Issue.7 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 29
    • 0034710619 scopus 로고    scopus 로고
    • Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1
    • E. Odintsova, T. Sugiura, and F. Berditchevski Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1 Curr. Biol. 10 16 2000 1009 1012
    • (2000) Curr. Biol. , vol.10 , Issue.16 , pp. 1009-1012
    • Odintsova, E.1    Sugiura, T.2    Berditchevski, F.3
  • 30
    • 4143061388 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions
    • D. Perez-Caballero, T. Hatziioannou, J. Martin-Serrano, and P.D. Bieniasz Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions J. Virol. 78 17 2004 9560 9563
    • (2004) J. Virol. , vol.78 , Issue.17 , pp. 9560-9563
    • Perez-Caballero, D.1    Hatziioannou, T.2    Martin-Serrano, J.3    Bieniasz, P.D.4
  • 32
    • 85047690554 scopus 로고    scopus 로고
    • Dangerous liaisons at the virological synapse
    • V. Piguet, and Q. Sattentau Dangerous liaisons at the virological synapse J. Clin. Invest. 114 2004 605 610
    • (2004) J. Clin. Invest. , vol.114 , pp. 605-610
    • Piguet, V.1    Sattentau, Q.2
  • 33
    • 0034715523 scopus 로고    scopus 로고
    • Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission
    • C. Pique, C. Lagaudriere-Gesbert, L. Delamarre, A.R. Rosenberg, H. Conjeaud, and M.C. Dokhelar Interaction of CD82 tetraspanin proteins with HTLV-1 envelope glycoproteins inhibits cell-to-cell fusion and virus transmission Virology 276 2 2000 455 465
    • (2000) Virology , vol.276 , Issue.2 , pp. 455-465
    • Pique, C.1    Lagaudriere-Gesbert, C.2    Delamarre, L.3    Rosenberg, A.R.4    Conjeaud, H.5    Dokhelar, M.C.6
  • 34
    • 0034744302 scopus 로고    scopus 로고
    • The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation
    • F. Rayne, F. Bouamr, J. Lalanne, and R.Z. Mamoun The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation J. Virol. 75 11 2001 5277 5287
    • (2001) J. Virol. , vol.75 , Issue.11 , pp. 5277-5287
    • Rayne, F.1    Bouamr, F.2    Lalanne, J.3    Mamoun, R.Z.4
  • 35
    • 5144222004 scopus 로고    scopus 로고
    • In vivo homodimerisation of HTLV-1 Gag and MA gives clues to the retroviral capsid and TM envelope protein arrangement
    • F. Rayne, A.V. Kajava, J. Lalanne, and R.Z. Mamoun In vivo homodimerisation of HTLV-1 Gag and MA gives clues to the retroviral capsid and TM envelope protein arrangement J. Mol. Biol. 343 4 2004 903 916
    • (2004) J. Mol. Biol. , vol.343 , Issue.4 , pp. 903-916
    • Rayne, F.1    Kajava, A.V.2    Lalanne, J.3    Mamoun, R.Z.4
  • 36
    • 0036644069 scopus 로고    scopus 로고
    • TCR engagement induces proline-rich tyrosine kinase-2 (Pyk2) translocation to the T cell-APC interface independently of Pyk2 activity and in an immunoreceptor tyrosine-based activation motif-mediated fashion
    • D. Sancho, M.C. Montoya, A. Monjas, M. Gordon-Alonso, T. Katagiri, D. Gil, R. Tejedor, B. Alarcon, and F. Sanchez-Madrid TCR engagement induces proline-rich tyrosine kinase-2 (Pyk2) translocation to the T cell-APC interface independently of Pyk2 activity and in an immunoreceptor tyrosine-based activation motif-mediated fashion J. Immunol. 169 1 2002 292 300
    • (2002) J. Immunol. , vol.169 , Issue.1 , pp. 292-300
    • Sancho, D.1    Montoya, M.C.2    Monjas, A.3    Gordon-Alonso, M.4    Katagiri, T.5    Gil, D.6    Tejedor, R.7    Alarcon, B.8    Sanchez-Madrid, F.9
  • 37
    • 0031971539 scopus 로고    scopus 로고
    • Functional analysis of CD82 in the early phase of T cell activation: Roles in cell adhesion and signal transduction
    • N. Shibagaki, K. Hanada, S. Yamaguchi, H. Yamashita, S. Shimada, and H. Hamada Functional analysis of CD82 in the early phase of T cell activation: roles in cell adhesion and signal transduction Eur. J. Immunol. 28 4 1998 1125 1133
    • (1998) Eur. J. Immunol. , vol.28 , Issue.4 , pp. 1125-1133
    • Shibagaki, N.1    Hanada, K.2    Yamaguchi, S.3    Yamashita, H.4    Shimada, S.5    Hamada, H.6
  • 38
    • 0032709802 scopus 로고    scopus 로고
    • Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: Functional association between CD82 and LFA-1 in T cell activation
    • N. Shibagaki, K. Hanada, H. Yamashita, S. Shimada, and H. Hamada Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation Eur. J. Immunol. 29 12 1999 4081 4091
    • (1999) Eur. J. Immunol. , vol.29 , Issue.12 , pp. 4081-4091
    • Shibagaki, N.1    Hanada, K.2    Yamashita, H.3    Shimada, S.4    Hamada, H.5
  • 39
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
    • C.S. Stipp, T.V. Kolesnikova, and M.E. Hemler EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily J. Biol. Chem. 276 44 2001 40545 40554
    • (2001) J. Biol. Chem. , vol.276 , Issue.44 , pp. 40545-40554
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 40
    • 0035895876 scopus 로고    scopus 로고
    • FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
    • C.S. Stipp, D. Orlicky, and M.E. Hemler FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein J. Biol. Chem. 276 7 2001 4853 4862
    • (2001) J. Biol. Chem. , vol.276 , Issue.7 , pp. 4853-4862
    • Stipp, C.S.1    Orlicky, D.2    Hemler, M.E.3
  • 43
    • 8144230161 scopus 로고    scopus 로고
    • Tetraspanin microdomains in immune cell signalling and malignant disease
    • M.D. Wright, G.W. Moseley, and A.B. van Spriel Tetraspanin microdomains in immune cell signalling and malignant disease Tissue Antigens 64 5 2004 533 542
    • (2004) Tissue Antigens , vol.64 , Issue.5 , pp. 533-542
    • Wright, M.D.1    Moseley, G.W.2    Van Spriel, A.B.3
  • 44
    • 0037409387 scopus 로고    scopus 로고
    • Tetraspanin proteins as organisers of membrane microdomains and signalling complexes
    • M. Yunta, and P.A. Lazo Tetraspanin proteins as organisers of membrane microdomains and signalling complexes Cell Signalling 15 6 2003 559 564
    • (2003) Cell Signalling , vol.15 , Issue.6 , pp. 559-564
    • Yunta, M.1    Lazo, P.A.2
  • 45
    • 0035816663 scopus 로고    scopus 로고
    • Transmembrane-4 superfamily proteins associate with activated protein kinase C (PKC) and link PKC to specific beta(1) integrins
    • X.A. Zhang, A.L. Bontrager, and M.E. Hemler Transmembrane-4 superfamily proteins associate with activated protein kinase C (PKC) and link PKC to specific beta(1) integrins J. Biol. Chem. 276 27 2001 25005 25013
    • (2001) J. Biol. Chem. , vol.276 , Issue.27 , pp. 25005-25013
    • Zhang, X.A.1    Bontrager, A.L.2    Hemler, M.E.3
  • 46
    • 0038179866 scopus 로고    scopus 로고
    • EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells
    • X.A. Zhang, W.S. Lane, S. Charrin, E. Rubinstein, and L. Liu EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells Cancer Res. 63 10 2003 2665 2674
    • (2003) Cancer Res. , vol.63 , Issue.10 , pp. 2665-2674
    • Zhang, X.A.1    Lane, W.S.2    Charrin, S.3    Rubinstein, E.4    Liu, L.5


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