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Volumn 21, Issue 22, 2002, Pages 5985-5995

Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules

Author keywords

CD2; GYF domain; Lipid rafts; NMR; SH3 domain

Indexed keywords

ARTICLE; BINDING AFFINITY; CELL FRACTIONATION; CHROMOSOME TRANSLOCATION; CYTOKINE PRODUCTION; CYTOPLASM; EXTRACELLULAR MATRIX; HYDROPHOBICITY; IMMUNOPRECIPITATION; MOLECULAR MODEL; PHYLOGENY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; SEQUENCE ANALYSIS; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; WESTERN BLOTTING;

EID: 0037112758     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf602     Document Type: Article
Times cited : (76)

References (39)
  • 2
    • 0034717290 scopus 로고    scopus 로고
    • Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains
    • Bedford, M.T., Frankel, A., Yaffe, M.B., Clarke, S., Leder, P. and Richard, S. (2000) Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains. J. Biol. Chem., 275, 16030-16036.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16030-16036
    • Bedford, M.T.1    Frankel, A.2    Yaffe, M.B.3    Clarke, S.4    Leder, P.5    Richard, S.6
  • 4
    • 0027988814 scopus 로고
    • The WW domain: A signalling site in dystrophin?
    • Bork, P. and Sudol, M. (1994) The WW domain: A signalling site in dystrophin? Trends Biochem. Sci., 19, 531-533.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 531-533
    • Bork, P.1    Sudol, M.2
  • 6
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson, L., Nystrom, L.E., Sundkvist, I., Markey, F. and Lindberg, U. (1977) Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J. Mol. Biol., 115, 465-483.
    • (1977) J. Mol. Biol. , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 7
    • 0003655830 scopus 로고    scopus 로고
    • University of California, San Francisco, CA
    • Case, D.A. et al. (1997) AMBER5. University of California, San Francisco, CA.
    • (1997) AMBER5
    • Case, D.A.1
  • 9
    • 0032483559 scopus 로고    scopus 로고
    • A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts
    • Dustin, M.L. et al. (1998) A novel adaptor protein orchestrates receptor patterning and cytoskeletal polarity in T-cell contacts. Cell, 94, 667-677.
    • (1998) Cell , vol.94 , pp. 667-677
    • Dustin, M.L.1
  • 10
    • 0028337397 scopus 로고
    • Structure of the regulatory domains of the Src-family tyrosine kinase Lck
    • Eck, M.J., Atwell, S.K., Shoelson, S.E. and Harrison, S.C. (1994) Structure of the regulatory domains of the Src-family tyrosine kinase Lck. Nature, 368, 764-769.
    • (1994) Nature , vol.368 , pp. 764-769
    • Eck, M.J.1    Atwell, S.K.2    Shoelson, S.E.3    Harrison, S.C.4
  • 11
    • 0032985562 scopus 로고    scopus 로고
    • The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences
    • Freund, C., Dotsch, V., Nishizawa, K., Reinherz, E.L. and Wagner, G. (1999) The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nat. Struct. Biol., 6, 656-660.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 656-660
    • Freund, C.1    Dotsch, V.2    Nishizawa, K.3    Reinherz, E.L.4    Wagner, G.5
  • 15
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P. and Simons, K. (1998) Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol., 141, 929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 16
    • 0027673371 scopus 로고
    • A new approach to the display of lipophilicity/hydrophilicity mapped on molecular surfaces
    • Heiden, W., Moeckel, G. and Brickmann, J. (1993) A new approach to the display of lipophilicity/hydrophilicity mapped on molecular surfaces. J. Comput. Aided Mol. Design, 7, 503-514.
    • (1993) J. Comput. Aided Mol. Design , vol.7 , pp. 503-514
    • Heiden, W.1    Moeckel, G.2    Brickmann, J.3
  • 17
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., Irving, B.A., van Oers, N.S., Chan, A.C. and Weiss, A. (1994) Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science, 263, 1136-1139.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.3    Chan, A.C.4    Weiss, A.5
  • 18
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B.K., Williamson, M.P. and Sudol, M. (2000) The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J., 14, 231-241.
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 19
    • 0027986678 scopus 로고
    • Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif
    • Koegl, M., Zlatkine, P., Ley, S.C., Courtneidge, S.A. and Magee, A.I. (1994) Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif. Biochem. J. 303, 749-753.
    • (1994) Biochem. J. , vol.303 , pp. 749-753
    • Koegl, M.1    Zlatkine, P.2    Ley, S.C.3    Courtneidge, S.A.4    Magee, A.I.5
  • 20
    • 0032535449 scopus 로고    scopus 로고
    • A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion
    • Li, J., Nishizawa, K., An, W., Hussey, R.E., Lialios, F.E., Salgia, R., Sunder-Plassmann, R. and Reinherz, E.L. (1998) A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion. EMBO J., 17, 7320-7336.
    • (1998) EMBO J. , vol.17 , pp. 7320-7336
    • Li, J.1    Nishizawa, K.2    An, W.3    Hussey, R.E.4    Lialios, F.E.5    Salgia, R.6    Sunder-Plassmann, R.7    Reinherz, E.L.8
  • 21
    • 0032584738 scopus 로고    scopus 로고
    • Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain
    • Lin, H., Hutchcroft, J.E., Andoniou, C.E., Kamoun, M., Band, H. and Bierer, B.E. (1998) Association of p59(fyn) with the T lymphocyte costimulatory receptor CD2. Binding of the Fyn Src homology (SH) 3 domain is regulated by the Fyn SH2 domain. J. Biol. Chem., 273, 19914-19921.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19914-19921
    • Lin, H.1    Hutchcroft, J.E.2    Andoniou, C.E.3    Kamoun, M.4    Band, H.5    Bierer, B.E.6
  • 22
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • Lu, P.J., Zhou, X.Z., Shen, M. and Lu, K.P. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science, 283, 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 23
    • 0023864050 scopus 로고
    • A novel viral oncogene with structural similarity to phospholipase C
    • Mayer, B.J., Hamaguchi, M. and Hanafusa, H. (1988) A novel viral oncogene with structural similarity to phospholipase C. Nature, 332, 272-275.
    • (1988) Nature , vol.332 , pp. 272-275
    • Mayer, B.J.1    Hamaguchi, M.2    Hanafusa, H.3
  • 24
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio, A., Saraste, M. and Wilmanns, M. (1994) High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat. Struct. Biol., 1, 546-551.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 25
    • 0030864520 scopus 로고    scopus 로고
    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr, K. et al. (1997) A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J., 16, 5433-5444.
    • (1997) EMBO J. , vol.16 , pp. 5433-5444
    • Niebuhr, K.1
  • 26
    • 0032441151 scopus 로고    scopus 로고
    • Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation
    • Nishizawa, K., Freund, C., Li, J., Wagner, G. and Reinherz, E.L. (1998) Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation. Proc. Natl Acad. Sci. USA, 95, 14897-14902.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14897-14902
    • Nishizawa, K.1    Freund, C.2    Li, J.3    Wagner, G.4    Reinherz, E.L.5
  • 27
    • 0034708444 scopus 로고    scopus 로고
    • Comparative genomics of the eukaryotes
    • Rubin, G.M. et al. (2000) Comparative genomics of the eukaryotes. Science, 287, 2204-2215.
    • (2000) Science , vol.287 , pp. 2204-2215
    • Rubin, G.M.1
  • 28
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J., Milpetz, F., Bork, P. and Ponting, C.P. (1998) SMART, a simple modular architecture research tool: Identification of signaling domains. Proc. Natl Acad. Sci. USA, 95, 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 29
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., Dietzen, D.J., Kwong, J., Link, D.C. and Lublin, D.M. (1994) Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. J. Cell Biol., 126, 353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 30
  • 31
    • 0023860445 scopus 로고
    • Sequence similarity of phospholipase C with the non-catalytic region of src
    • Stahl, M.L., Ferenz, C.R., Kelleher, K.L., Kriz, R.W. and Knopf, J.L. (1988) Sequence similarity of phospholipase C with the non- catalytic region of src. Nature, 332, 269-272.
    • (1988) Nature , vol.332 , pp. 269-272
    • Stahl, M.L.1    Ferenz, C.R.2    Kelleher, K.L.3    Kriz, R.W.4    Knopf, J.L.5
  • 32
    • 0032508408 scopus 로고    scopus 로고
    • lck-independent pathway of CD2 signaling involves Jun kinase
    • lck-independent pathway of CD2 signaling involves Jun kinase. J. Biol. Chem., 273, 24249-24257.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24249-24257
    • Sunder-Plassmann, R.1    Reinherz, E.L.2
  • 33
    • 84866476582 scopus 로고    scopus 로고
    • 2-terminal myristoylation and palmitoylation at cysteine-3
    • 2-terminal myristoylation and palmitoylation at cysteine-3. J. Cell Biol., 136, 1023-1035.
    • (1997) J. Cell Biol. , vol.136 , pp. 1023-1035
    • Van't Hof, W.1    Resh, M.D.2
  • 34
    • 0033037036 scopus 로고    scopus 로고
    • Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors
    • Wang, J.H., Smolyar, A., Tan, K., Liu, J.H., Kim, M., Sun, Z.Y., Wagner, G. and Reinherz, E.L. (1999) Structure of a heterophilic adhesion complex between the human CD2 and CD58 (LFA-3) counterreceptors. Cell, 97, 791-803
    • (1999) Cell , vol.97 , pp. 791-803
    • Wang, J.H.1    Smolyar, A.2    Tan, K.3    Liu, J.H.4    Kim, M.5    Sun, Z.Y.6    Wagner, G.7    Reinherz, E.L.8
  • 36
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C. and Seed, B. (1998) Membrane compartmentation is required for efficient T cell activation. Immunity, 8, 723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 37
    • 0035380477 scopus 로고    scopus 로고
    • Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction
    • Yang, H. and Reinherz, E.L. (2001) Dynamic recruitment of human CD2 into lipid rafts. Linkage to T cell signal transduction. J. Biol. Chem., 276, 18775-18785.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18775-18785
    • Yang, H.1    Reinherz, E.L.2
  • 38
    • 0013484134 scopus 로고
    • Structural basis for the binding of proline-rich peptides to SH3 domains
    • Yu, H., Chen, J.K., Feng, S., Dalgarno, D.C., Brauer, A.W. and Schreiber, S.L. (1994) Structural basis for the binding of proline-rich peptides to SH3 domains. Cell, 76, 933-945.
    • (1994) Cell , vol.76 , pp. 933-945
    • Yu, H.1    Chen, J.K.2    Feng, S.3    Dalgarno, D.C.4    Brauer, A.W.5    Schreiber, S.L.6
  • 39
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., Trible, R.P. and Samelson, L.E. (1998) LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity, 9, 239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.