메뉴 건너뛰기




Volumn 145, Issue 2, 2000, Pages 377-389

Dual fatty acylation of p59(Fyn) is required for association with the T cell receptor ζ chain through phosphotyrosine-Src homology domain-2 interactions

Author keywords

Acylation; Cell membrane; Protein tyrosine kinase; Receptor antigen; Src homology domains

Indexed keywords

CD8 ANTIGEN; PROTEIN KINASE P60; PROTEIN N MYRISTOYLTRANSFERASE; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 0344348996     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.145.2.377     Document Type: Article
Times cited : (104)

References (46)
  • 3
    • 0029145798 scopus 로고
    • Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristylated proteins
    • Berthiaume, L., and M.D. Resh. 1995. Biochemical characterization of a palmitoyl acyltransferase activity that palmitoylates myristylated proteins. J. Biol. Chem. 270:22399-22405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22399-22405
    • Berthiaume, L.1    Resh, M.D.2
  • 4
    • 0030939784 scopus 로고    scopus 로고
    • Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4
    • Bijlmakers, M.J., M. Isobe-Nakamura, L.J. Ruddock, and M. Marsh. 1997. Intrinsic signals in the unique domain target p56(lck) to the plasma membrane independently of CD4. J. Cell Biol. 137:1029-1040.
    • (1997) J. Cell Biol. , vol.137 , pp. 1029-1040
    • Bijlmakers, M.J.1    Isobe-Nakamura, M.2    Ruddock, L.J.3    Marsh, M.4
  • 5
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A., and E. London. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol. 14:111-136.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 7
    • 0029007283 scopus 로고
    • Cell-surface-expressed T-cell antigen-receptor zeta chain is associated with the cytoskeleton
    • Caplan, S., S. Zeliger, L. Wang, and M. Baniyash. 1995. Cell-surface-expressed T-cell antigen-receptor zeta chain is associated with the cytoskeleton. Proc. Natl. Acad. Sci. USA. 92:4768-4772.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4768-4772
    • Caplan, S.1    Zeliger, S.2    Wang, L.3    Baniyash, M.4
  • 9
    • 0026544934 scopus 로고
    • Mutations of human myristoyl-CoA: Protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in saccharomyces cerevisiae
    • Duriono, R.J., S.I. Reed, and J.I. Gordon. 1992. Mutations of human myristoyl-CoA: protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 89:4129-4133.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4129-4133
    • Duriono, R.J.1    Reed, S.I.2    Gordon, J.I.3
  • 10
    • 0026459940 scopus 로고
    • p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain
    • Gauen, L.K.T., A.-N.T. Kong, L.E. Samelson, and A.S. Shaw. 1992. p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain. Mol. Cell. Biol. 12:5438-5446.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5438-5446
    • Gauen, L.K.T.1    Kong, A.-N.T.2    Samelson, L.E.3    Shaw, A.S.4
  • 11
    • 0030162958 scopus 로고    scopus 로고
    • Multiple features of the p59fyn src homology 4 domain define a motif for immune-receptor tyrosine-based activation motif (ITAM) binding and for plasma membrane localization
    • Gauen, L.K.T., M.E. Linder, and A.S. Shaw. 1996. Multiple features of the p59fyn src homology 4 domain define a motif for immune-receptor tyrosine-based activation motif (ITAM) binding and for plasma membrane localization. J. Cell Biol. 133:1007-1015.
    • (1996) J. Cell Biol. , vol.133 , pp. 1007-1015
    • Gauen, L.K.T.1    Linder, M.E.2    Shaw, A.S.3
  • 13
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyltransferase
    • Giang, D.K., and B.F. Cravatt. 1998. A second mammalian N-myristoyltransferase. J. Biol. Chem. 273:6595-6598.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 14
    • 0030657584 scopus 로고    scopus 로고
    • Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
    • Glover, C.J., K.D. Hartman, and R.L. Felsted. 1997. Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction. J. Biol. Chem. 272:28680-28689.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28680-28689
    • Glover, C.J.1    Hartman, K.D.2    Felsted, R.L.3
  • 15
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock, J.F., H. Paterson, and C.J. Marshall. 1990. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell. 63:133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 16
    • 0026064305 scopus 로고
    • The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways
    • Irving, B.A., and A. Weiss. 1991. The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways. Cell. 64:891-901.
    • (1991) Cell , vol.64 , pp. 891-901
    • Irving, B.A.1    Weiss, A.2
  • 18
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK prolein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis, P.S., A.I. Magee, and S.C. Ley. 1997. S-acylation of LCK prolein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO (Eur. Mol. Biol. Organ.) J. 16:4983-4998.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 19
    • 0024023829 scopus 로고
    • The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: Lysine 7 is a critical determinant
    • Kaplan, J.M., G. Mardon, J.M. Bishop, and H.E. Varmus. 1988. The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant. Mol. Cell. Biol. 8:2435-2441.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2435-2441
    • Kaplan, J.M.1    Mardon, G.2    Bishop, J.M.3    Varmus, H.E.4
  • 21
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li, X., and Y.-H. Chang. 1995. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl. Acad. Sci. USA. 92:12357-12361.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.-H.2
  • 22
    • 0032559586 scopus 로고    scopus 로고
    • Cytoskelelal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motif-dependent mechanism
    • Lowin-Kropf, B., V. Smith Shapiro, and A. Weiss. 1998. Cytoskelelal polarization of T cells is regulated by an immunoreceptor tyrosine-based activation motif-dependent mechanism. J. Cell Biol. 140:861-871.
    • (1998) J. Cell Biol. , vol.140 , pp. 861-871
    • Lowin-Kropf, B.1    Smith Shapiro, V.2    Weiss, A.3
  • 23
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts
    • Melkonian, K.A., A.G. Ostermeyer, J.Z. Chen, M.G. Roth, and D.A. Brown. 1999. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. J. Biol. Chem. 274:3910-3917.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 26
    • 0028970587 scopus 로고
    • p80/85 cortactin associates with the Src SH2 domain and colocalizes with v-Src in transformed cells
    • Okamura, H., and M.D. Resh. 1995. p80/85 Cortactin associates with the Src SH2 domain and colocalizes with v-Src in transformed cells. J. Biol. Chem. 270:26613-26618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26613-26618
    • Okamura, H.1    Resh, M.D.2
  • 27
    • 0025245802 scopus 로고
    • Metabolic activation of 2-substituted derivates of myrisitic acid to form potent inhibitors of myristoyl CoA:Protein N-myristoyltransferase
    • Paige, L.A., G. Zheng, S.A. DeFrees, J.M. Cassady, and R.J. Gaehlen. 1990. Metabolic activation of 2-substituted derivates of myrisitic acid to form potent inhibitors of myristoyl CoA:protein N-myristoyltransferase. Biochemistry. 29:10566-10573.
    • (1990) Biochemistry , vol.29 , pp. 10566-10573
    • Paige, L.A.1    Zheng, G.2    Defrees, S.A.3    Cassady, J.M.4    Gaehlen, R.J.5
  • 28
    • 0028072831 scopus 로고
    • Fatty acyl transfer by human N-myristyl transferase is dependent upon conserved cysteine and hislidine residues
    • Peseckis, S.M., and M.D. Resh. 1994. Fatty acyl transfer by human N-myristyl transferase is dependent upon conserved cysteine and hislidine residues. J. Biol. Chem. 269:30888-30892.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30888-30892
    • Peseckis, S.M.1    Resh, M.D.2
  • 30
    • 0027772325 scopus 로고
    • Interaction of tyrosine kinase oncoproteins with cellular membranes
    • Resh, M.D. 1993. Interaction of tyrosine kinase oncoproteins with cellular membranes. Biochim. Biophys. Acta. 1155:307-322.
    • (1993) Biochim. Biophys. Acta. , vol.1155 , pp. 307-322
    • Resh, M.D.1
  • 31
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh, M.D. 1994. Myristylation and palmitylation of Src family members: the fats of the matter. Cell. 76:411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 32
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh, M.D. 1996. Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins. Cell. Signalling. 8:403-412.
    • (1996) Cell. Signalling , vol.8 , pp. 403-412
    • Resh, M.D.1
  • 33
  • 34
    • 0026499534 scopus 로고
    • Characterization of the T cell antigen receptor p60fyn protein tyrosine kinase association by chemical cross-linking
    • Sarosi, G.A., P.M. Thomas, M. Egerton, A.F. Phillips, K.W. Kim, E. Bonvini, and L.E. Samelson. 1992. Characterization of the T cell antigen receptor p60fyn protein tyrosine kinase association by chemical cross-linking. Int. Immunol. 4:1211-1217.
    • (1992) Int. Immunol. , vol.4 , pp. 1211-1217
    • Sarosi, G.A.1    Thomas, P.M.2    Egerton, M.3    Phillips, A.F.4    Kim, K.W.5    Bonvini, E.6    Samelson, L.E.7
  • 35
    • 0028175989 scopus 로고
    • Cysteine 3 of Src family protein tyrosine kinases determines palmitoylalion and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwong, D.C. Link, and D.M. Lublin. 1994. Cysteine 3 of Src family protein tyrosine kinases determines palmitoylalion 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
  • 37
    • 0027615718 scopus 로고
    • Members of the src family of nonreceplor tyrosine kinases share a common mechanism for membrane binding
    • Silverman, L., M. Sudol, and M.D. Resh. 1993. Members of the src family of nonreceplor tyrosine kinases share a common mechanism for membrane binding. Cell Growth Differ. 4:475-482.
    • (1993) Cell Growth Differ. , vol.4 , pp. 475-482
    • Silverman, L.1    Sudol, M.2    Resh, M.D.3
  • 38
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 39
    • 0026684621 scopus 로고
    • The glycophosphatidylinositol-anchored Thy-1 molecule interacts with the p60fyn protein tyrosine kinase in T cells
    • Thomas, P.M., and L.E. Samelson. 1992. The glycophosphatidylinositol-anchored Thy-1 molecule interacts with the p60fyn protein tyrosine kinase in T cells. J. Biol. Chem. 267:12317-12322.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12317-12322
    • Thomas, P.M.1    Samelson, L.E.2
  • 40
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas, S.M., and J.S. Brugge. 1997. Cellular functions regulated by Src family kinases. Annu. Rev. Cell. Dev. Biol. 13:513-609.
    • (1997) Annu. Rev. Cell. Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 41
    • 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
  • 42
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox, C., J.-S. Hu, and E.N. Olson. 1987. Acylation of proteins with myristic acid occurs cotranslationally. Science. 238:1275-1278.
    • (1987) Science. , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.-S.2    Olson, E.N.3
  • 44
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., T. Brennan, O Li, C. McCormack, and B. Seed. 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, O.3    McCormack, C.4    Seed, B.5
  • 45
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., R.P. Trible, and L.E. Samelson. 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
  • 46
    • 0030948362 scopus 로고    scopus 로고
    • Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif
    • Zlatkine, P., B. Mehul, and A.I. Magee. 1997. Retargeting of cytosolic proteins to the plasma membrane by the Lck protein tyrosine kinase dual acylation motif. J. Cell Sci. 110:673-679.
    • (1997) J. Cell Sci. , vol.110 , pp. 673-679
    • Zlatkine, P.1    Mehul, B.2    Magee, A.I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.