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Volumn 172, Issue 11, 2004, Pages 6902-6912

Molecular determinants regulating the pairing of NKG2 molecules with CD94 for cell surface heterodimer expression

Author keywords

[No Author keywords available]

Indexed keywords

CD94 ANTIGEN; CELL RECEPTOR; NATURAL KILLER CELL RECEPTOR NKG2C; NATURAL KILLER CELL RECEPTOR NKG2D; UNCLASSIFIED DRUG;

EID: 2442670329     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.172.11.6902     Document Type: Article
Times cited : (14)

References (45)
  • 3
    • 0036644075 scopus 로고    scopus 로고
    • NK cell receptors of the orangutan (Pongo pygmaeus): A pivotal species for tracking the coevolution of killer cell Ig-like receptors with MHC-C
    • Guethlein, L. A., L. R. Flodin, E. J. Adams, and P. Parham. 2002. NK cell receptors of the orangutan (Pongo pygmaeus): a pivotal species for tracking the coevolution of killer cell Ig-like receptors with MHC-C. J. Immunol. 169:220.
    • (2002) J. Immunol. , vol.169 , pp. 220
    • Guethlein, L.A.1    Flodin, L.R.2    Adams, E.J.3    Parham, P.4
  • 4
    • 0025754310 scopus 로고
    • DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells
    • Houchins, J. P., T. Yabe, C. McSherry, and F. H. Bach. 1991. DNA sequence analysis of NKG2, a family of related cDNA clones encoding type II integral membrane proteins on human natural killer cells. J. Exp. Med. 173:1017.
    • (1991) J. Exp. Med. , vol.173 , pp. 1017
    • Houchins, J.P.1    Yabe, T.2    McSherry, C.3    Bach, F.H.4
  • 5
    • 0033025724 scopus 로고    scopus 로고
    • Cloning of murine NKG2A, B and C: Second family of C-type lectin receptors on murine NK cells
    • Lohwasser, S., P. Hande, D. L. Mager, and F. Takei. 1999. Cloning of murine NKG2A, B and C: second family of C-type lectin receptors on murine NK cells. Eur. J. Immunol. 29:755.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 755
    • Lohwasser, S.1    Hande, P.2    Mager, D.L.3    Takei, F.4
  • 7
    • 0034022632 scopus 로고    scopus 로고
    • Characterization of rhesus monkey CD94/NKG2 family members and identification of novel transmembrane-deleted forms of NKG2-A, B, C, and D
    • LaBonte, M. L., D. B. Levy, and N. L. Letvin. 2000. Characterization of rhesus monkey CD94/NKG2 family members and identification of novel transmembrane-deleted forms of NKG2-A, B, C, and D. Immunogenetics 51:496.
    • (2000) Immunogenetics , vol.51 , pp. 496
    • LaBonte, M.L.1    Levy, D.B.2    Letvin, N.L.3
  • 8
    • 0035664414 scopus 로고    scopus 로고
    • The KIR and CD94/NKG2 families of molecules in the rhesus monkey
    • LaBonte, M. L., M. L. Hershberger, B. Korber, and N. L. Letvin. 2001. The KIR and CD94/NKG2 families of molecules in the rhesus monkey. Immunol. Rev. 183:25.
    • (2001) Immunol. Rev. , vol.183 , pp. 25
    • LaBonte, M.L.1    Hershberger, M.L.2    Korber, B.3    Letvin, N.L.4
  • 10
    • 0030217971 scopus 로고    scopus 로고
    • CD94 and a novel associated protein (94AP) form a NK cell receptor involved in the recognition of HLA-A, HLA-B, and HLA-C allotypes
    • Phillips, J. H., C. Chang, J. Mattson, J. E. Gumperz, P. Parham, and L. L. Lanier. 1996. CD94 and a novel associated protein (94AP) form a NK cell receptor involved in the recognition of HLA-A, HLA-B, and HLA-C allotypes. Immunity 5:163.
    • (1996) Immunity , vol.5 , pp. 163
    • Phillips, J.H.1    Chang, C.2    Mattson, J.3    Gumperz, J.E.4    Parham, P.5    Lanier, L.L.6
  • 11
    • 0030470555 scopus 로고    scopus 로고
    • Human natural killer cell receptors involved in MHC class I recognition are disulfide-linked heterodimers of CD94 and NKG2 subunits
    • Lazetic, S., C. Chang, J. P. Houchins, L. L. Lanier, and J. H. Phillips. 1996. Human natural killer cell receptors involved in MHC class I recognition are disulfide-linked heterodimers of CD94 and NKG2 subunits. J. Immunol. 157:4741.
    • (1996) J. Immunol. , vol.157 , pp. 4741
    • Lazetic, S.1    Chang, C.2    Houchins, J.P.3    Lanier, L.L.4    Phillips, J.H.5
  • 13
    • 0031960065 scopus 로고    scopus 로고
    • Specific engagement of the CD94/NKG2-A killer inhibitory receptor by the HLA-E class Ib molecule induces SHP-1 phosphatase recruitment to tyrosine-phosphorylated NKG2-A: Evidence for receptor function in heterologous transfectants
    • Carretero, M., G. Palmieri, M. Llano, V. Tullio, A. Santoni, D. E. Geraghty, and M. Lopez-Botet. 1998, Specific engagement of the CD94/NKG2-A killer inhibitory receptor by the HLA-E class Ib molecule induces SHP-1 phosphatase recruitment to tyrosine-phosphorylated NKG2-A: evidence for receptor function in heterologous transfectants. Eur. J. Immunol. 28:1280.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 1280
    • Carretero, M.1    Palmieri, G.2    Llano, M.3    Tullio, V.4    Santoni, A.5    Geraghty, D.E.6    Lopez-Botet, M.7
  • 14
    • 2642611958 scopus 로고    scopus 로고
    • Inhibition of antigen-induced T cell response and antibody-induced NK cell cytotoxicity by NKG2A: Association of NKG2A with SHP-1 and SHP-2 protein-tyrosine phosphatases
    • Le Drean, E., F. Vely, L. Olcese, A. Cambiaggi, S. Guia, G. Krystal, N. Gervois, A. Moretta, F. Jotereau, and E. Vivier. 1998. Inhibition of antigen-induced T cell response and antibody-induced NK cell cytotoxicity by NKG2A: association of NKG2A with SHP-1 and SHP-2 protein-tyrosine phosphatases. Eur. J. Immunol. 28:264.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 264
    • Le Drean, E.1    Vely, F.2    Olcese, L.3    Cambiaggi, A.4    Guia, S.5    Krystal, G.6    Gervois, N.7    Moretta, A.8    Jotereau, F.9    Vivier, E.10
  • 15
    • 0031569525 scopus 로고    scopus 로고
    • Natural killer cell cytolytic activity is inhibited by NKG2-A and activated by NKG2-C
    • Houchins, J. P., L. L. Lanier, E. C. Niemi, J. H. Phillips, and J. C. Ryan. 1997. Natural killer cell cytolytic activity is inhibited by NKG2-A and activated by NKG2-C. J. Immunol. 158:3603.
    • (1997) J. Immunol. , vol.158 , pp. 3603
    • Houchins, J.P.1    Lanier, L.L.2    Niemi, E.C.3    Phillips, J.H.4    Ryan, J.C.5
  • 16
    • 0032510146 scopus 로고    scopus 로고
    • Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells
    • Lanier, L. L., B. C. Corliss, J. Wu, C. Leong, and J. H. Phillips. 1998. Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells. Nature 391:703.
    • (1998) Nature , vol.391 , pp. 703
    • Lanier, L.L.1    Corliss, B.C.2    Wu, J.3    Leong, C.4    Phillips, J.H.5
  • 17
    • 0034503091 scopus 로고    scopus 로고
    • The ITAM-bearing transmembrane adaptor DAP12 in lymphoid and myeloid cell function
    • Lanier, L. L., and A. B. H. Bakker. 2000. The ITAM-bearing transmembrane adaptor DAP12 in lymphoid and myeloid cell function. Immunol. Today 21:611.
    • (2000) Immunol. Today , vol.21 , pp. 611
    • Lanier, L.L.1    Bakker, A.B.H.2
  • 18
    • 0031692643 scopus 로고    scopus 로고
    • HLA-E-bound peptides influence recognition by inhibitory and triggering CD94/NKG2 receptors: Preferential response to an HLA-G-derived nonamer
    • Llano, M., N. Lee, F. Navarro, P. Garcia, J. P. Albar, D. E. Geraghty, and M. Lopez-Botet. 1998. HLA-E-bound peptides influence recognition by inhibitory and triggering CD94/NKG2 receptors: preferential response to an HLA-G-derived nonamer. Eur. J. Immunol. 28:2854.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 2854
    • Llano, M.1    Lee, N.2    Navarro, F.3    Garcia, P.4    Albar, J.P.5    Geraghty, D.E.6    Lopez-Botet, M.7
  • 21
    • 0033151621 scopus 로고    scopus 로고
    • The selective downregulation of class I major histocompatibility complex proteins by HIV-1 protects HIV-infected cells from NK cells
    • Cohen, G. B., R. T. Gandhi, D. M. Davis, O. Mandelboim, B. K. Chen, J. L. Strominger, and D. Baltimore. 1999. The selective downregulation of class I major histocompatibility complex proteins by HIV-1 protects HIV-infected cells from NK cells. Immunity 10:661.
    • (1999) Immunity , vol.10 , pp. 661
    • Cohen, G.B.1    Gandhi, R.T.2    Davis, D.M.3    Mandelboim, O.4    Chen, B.K.5    Strominger, J.L.6    Baltimore, D.7
  • 22
    • 0025066823 scopus 로고
    • Immunologic and pathologic manifestations of the infection of rhesus monkeys with simian immunodeficiency virus of macaques
    • Letvin, N. L., and N. W. King. 1990. Immunologic and pathologic manifestations of the infection of rhesus monkeys with simian immunodeficiency virus of macaques. J. Acquir. Immune Defic. Syndr. 3:1023.
    • (1990) J. Acquir. Immune Defic. Syndr. , vol.3 , pp. 1023
    • Letvin, N.L.1    King, N.W.2
  • 23
    • 0031711467 scopus 로고    scopus 로고
    • Pathogenesis of Lyme neuroborreliosis in the rhesus monkey: The early disseminated and chronic phases of disease in the peripheral nervous system
    • Roberts, E. D., R. P. J. Bohm, R. C. J. Lowrie, G. Habicht, L. Katona, J. Piesman, and M. T. Philipp. 1998. Pathogenesis of Lyme neuroborreliosis in the rhesus monkey: the early disseminated and chronic phases of disease in the peripheral nervous system. J. Infect. Dis. 178:722.
    • (1998) J. Infect. Dis. , vol.178 , pp. 722
    • Roberts, E.D.1    Bohm, R.P.J.2    Lowrie, R.C.J.3    Habicht, G.4    Katona, L.5    Piesman, J.6    Philipp, M.T.7
  • 25
    • 0032100703 scopus 로고    scopus 로고
    • Association of DAP12 with activating CD94/NKG2C NK cell receptors
    • Lanier, L. L., B. Corliss, J. Wu, and J. H. Phillips. 1998. Association of DAP12 with activating CD94/NKG2C NK cell receptors. Immunity 8:693.
    • (1998) Immunity , vol.8 , pp. 693
    • Lanier, L.L.1    Corliss, B.2    Wu, J.3    Phillips, J.H.4
  • 26
    • 0030695442 scopus 로고    scopus 로고
    • Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: A fluorescence resonance energy transfer study
    • Damjanovich, S., L. Bene, J. Matko, A. Alileche, G. K. Goldman, S. Sharrow, and T. A. Waldmann. 1997. Preassembly of interleukin 2 (IL-2) receptor subunits on resting Kit 225 K6 T cells and their modulation by IL-2, IL-7, and IL-15: a fluorescence resonance energy transfer study. Proc. Natl. Acad. Sci. USA 94:13134.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13134
    • Damjanovich, S.1    Bene, L.2    Matko, J.3    Alileche, A.4    Goldman, G.K.5    Sharrow, S.6    Waldmann, T.A.7
  • 27
    • 0035870746 scopus 로고    scopus 로고
    • The interacting domains of three MutL heterodimers in man: hMLH1 interacts with 36 homologous amino acid residues within hMLH3, hPMS1 and hPMS2
    • Kondo, E., A. Horii, and S. Fukushige. 2001. The interacting domains of three MutL heterodimers in man: hMLH1 interacts with 36 homologous amino acid residues within hMLH3, hPMS1 and hPMS2. Nucleic Acids Res. 29:1695.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1695
    • Kondo, E.1    Horii, A.2    Fukushige, S.3
  • 28
    • 0033575142 scopus 로고    scopus 로고
    • 2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis
    • 2-terminal BH4 domain of Bcl-2 is functional for heterodimerization with Bax and inhibition of apoptosis. J. Biol. Chem. 274:20415.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20415
    • Hirotani, M.1    Zhang, Y.2    Fujita, N.3    Naito, M.4    Tsuruo, T.5
  • 29
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki, M., R. J. Youle, and N. Tjandra. 2000. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 103:645.
    • (2000) Cell , vol.103 , pp. 645
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 30
    • 0029982848 scopus 로고    scopus 로고
    • Nuclear protein import: Ran-GTP dissociates the karyopherin αβ heterodimer by displacing α from an overlapping binding site on β
    • Moroianu, J., G. Blobel, and A. Radu. 1996. Nuclear protein import: Ran-GTP dissociates the karyopherin αβ heterodimer by displacing α from an overlapping binding site on β. Proc. Natl. Acad. Sci. USA 93:7059.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7059
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 32
    • 0034031173 scopus 로고    scopus 로고
    • Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins
    • Cocquerel, L., C. Wychowski, F. Minner, F. Penin, and J. Dubuisson. 2000. Charged residues in the transmembrane domains of hepatitis C virus glycoproteins play a major role in the processing, subcellular localization, and assembly of these envelope proteins. J. Virol. 74:3623.
    • (2000) J. Virol. , vol.74 , pp. 3623
    • Cocquerel, L.1    Wychowski, C.2    Minner, F.3    Penin, F.4    Dubuisson, J.5
  • 33
    • 0026485306 scopus 로고
    • Role of transmembrane domain interactions in the assembly of class II MHC molecules
    • Cosson, P., and J. Bonifacino. 1992. Role of transmembrane domain interactions in the assembly of class II MHC molecules. Science 258:659.
    • (1992) Science , vol.258 , pp. 659
    • Cosson, P.1    Bonifacino, J.2
  • 34
    • 0025819126 scopus 로고
    • Membrane protein association by potential intramembrane charge pairs
    • Cosson, P., S. P. Lankford, J. Bonifacino, and R. D. Klausner. 1991. Membrane protein association by potential intramembrane charge pairs. Nature 351.
    • (1991) Nature , pp. 351
    • Cosson, P.1    Lankford, S.P.2    Bonifacino, J.3    Klausner, R.D.4
  • 36
    • 0025761865 scopus 로고
    • Pair-wise, cooperative and inhibitory interactions describe the assembly and probable structure of the T-cell antigen receptor
    • Manolios, N., F. Letourneur, J. S. Bonifacino, and R. D. Klausner. 1991. Pair-wise, cooperative and inhibitory interactions describe the assembly and probable structure of the T-cell antigen receptor. EMBO J. 10:1643.
    • (1991) EMBO J. , vol.10 , pp. 1643
    • Manolios, N.1    Letourneur, F.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 37
    • 0027457742 scopus 로고
    • Transmembrane domain length affects charge-mediated retention degradation of proteins within the endoplasmic reticulum
    • Lankford, S. P., P. Cosson, J. S. Bonifacino, and R. D. Klausner. 1993. Transmembrane domain length affects charge-mediated retention degradation of proteins within the endoplasmic reticulum. J. Biol. Chem. 268:4814.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4814
    • Lankford, S.P.1    Cosson, P.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 38
    • 0034022205 scopus 로고    scopus 로고
    • Reconstitution of bacterial expressed human CD94: The importance of the stem region for dimer formation
    • Boyington, J. C., A. N. Raiz, A. G. Brooks, A. Patamawenu, and P. D. Sun. 2000. Reconstitution of bacterial expressed human CD94: the importance of the stem region for dimer formation. Protein Expr. Purif. 18:235.
    • (2000) Protein Expr. Purif. , vol.18 , pp. 235
    • Boyington, J.C.1    Raiz, A.N.2    Brooks, A.G.3    Patamawenu, A.4    Sun, P.D.5
  • 39
    • 0033053772 scopus 로고    scopus 로고
    • Structure of CD94 reveals a novel C-type lectin fold: Implications for the NK cell-associated CD94/NKG2 receptors
    • Boyington, J. C., A. N. Riaz, A. Patamawenu, J. E. Coligan, A. G. Brooks, and P. D. Sun. 1999. Structure of CD94 reveals a novel C-type lectin fold: implications for the NK cell-associated CD94/NKG2 receptors. Immunity 10:75.
    • (1999) Immunity , vol.10 , pp. 75
    • Boyington, J.C.1    Riaz, A.N.2    Patamawenu, A.3    Coligan, J.E.4    Brooks, A.G.5    Sun, P.D.6
  • 42
    • 0030266705 scopus 로고    scopus 로고
    • Clonotypic differences in signaling from CD94 (kp43) on NK cells lead to divergent cellular responses
    • Brumbaugh, K. M., J. J. Perez-Villar, C. J. Dick, R. A. Schoon, M. Lopez-Botet, and P. J. Leibson. 1996. Clonotypic differences in signaling from CD94 (kp43) on NK cells lead to divergent cellular responses. J. Immunol. 157:2804.
    • (1996) J. Immunol. , vol.157 , pp. 2804
    • Brumbaugh, K.M.1    Perez-Villar, J.J.2    Dick, C.J.3    Schoon, R.A.4    Lopez-Botet, M.5    Leibson, P.J.6
  • 43
    • 0036606062 scopus 로고    scopus 로고
    • Differential expression of inhibitory and activating CD94/NKG2 receptors on NK cell clones
    • Brostjan, C., T. Bellon, Y. Sobanov, M. Lopez-Botet, and E. Hofer. 2002. Differential expression of inhibitory and activating CD94/NKG2 receptors on NK cell clones. J. Immunol. Methods 264:109.
    • (2002) J. Immunol. Methods , vol.264 , pp. 109
    • Brostjan, C.1    Bellon, T.2    Sobanov, Y.3    Lopez-Botet, M.4    Hofer, E.5
  • 45
    • 0037093979 scopus 로고    scopus 로고
    • Orderly and nonstochastic acquisition of CD94/NKG2 receptors by developing NK cells derived from embryonic stem cells in vitro
    • Lian, R. H., M. Maeda, S. Lohwasser, M. Delcommenne, T. Nakano, R. E. Vance, D. H. Raulet, and F. Takei. 2002. Orderly and nonstochastic acquisition of CD94/NKG2 receptors by developing NK cells derived from embryonic stem cells in vitro. J. Immunol. 168:4980.
    • (2002) J. Immunol. , vol.168 , pp. 4980
    • Lian, R.H.1    Maeda, M.2    Lohwasser, S.3    Delcommenne, M.4    Nakano, T.5    Vance, R.E.6    Raulet, D.H.7    Takei, F.8


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