메뉴 건너뛰기




Volumn 8, Issue 5, 1997, Pages 843-854

pp60(v-src) transformation of rat cells but not chicken cells strongly correlates with low-affinity phosphopeptide binding by the SH2 domain

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PHOSPHOPEPTIDE; PROTEIN KINASE P60;

EID: 0030612112     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.5.843     Document Type: Article
Times cited : (3)

References (67)
  • 1
    • 0027436135 scopus 로고
    • Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides
    • Bibbins, K.B., Boeuf, H., and Varmus, H.E. (1993). Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides. Mol. Cell. Biol. 13, 7278-7287.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7278-7287
    • Bibbins, K.B.1    Boeuf, H.2    Varmus, H.E.3
  • 2
    • 0028894018 scopus 로고
    • Binding in vitro of phosphotyrosine-containing proteins to pp60(c-src) SH2 domain does not correlate with CEF cell transformation
    • Boeuf, H., Murphy, J., Bibbins, K.B., and Varmus, H.E. (1995). Binding in vitro of phosphotyrosine-containing proteins to pp60(c-src) SH2 domain does not correlate with CEF cell transformation. Oncogene 10, 433-438.
    • (1995) Oncogene , vol.10 , pp. 433-438
    • Boeuf, H.1    Murphy, J.2    Bibbins, K.B.3    Varmus, H.E.4
  • 4
    • 0000522346 scopus 로고
    • Retroviral vectors
    • ed. D.M. Glover, Oxford, United Kingdom: IRL Press
    • Brown, A.M.C., and Scott, M.R.D. (1987). Retroviral vectors. In: DNA Cloning, ed. D.M. Glover, Oxford, United Kingdom: IRL Press, 189-212.
    • (1987) DNA Cloning , pp. 189-212
    • Brown, A.M.C.1    Scott, M.R.D.2
  • 11
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • Cooper, J.A., and Howell, B. (1993). The when and how of Src regulation. Cell 73, 1051-1054.
    • (1993) Cell , vol.73 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 12
    • 0024537128 scopus 로고
    • Linker insertion-deletion mutagenesis of the v-src gene: Isolation of host- And temperature-defendent mutants
    • DeClue, J.E., and Martin, G.S. (1989). Linker insertion-deletion mutagenesis of the v-src gene: isolation of host-and temperature-defendent mutants. J. Virol. 63, 542-554.
    • (1989) J. Virol. , vol.63 , pp. 542-554
    • DeClue, J.E.1    Martin, G.S.2
  • 13
    • 0027502504 scopus 로고
    • Recognition of a high-affinity phosphotyrosyl peptide by the src homology-2 domain of p56(lck)
    • Eck, M.J., Shoelson, S.E., and Harrison, S.C. (1993). Recognition of a high-affinity phosphotyrosyl peptide by the src homology-2 domain of p56(lck). Nature 362, 87-91.
    • (1993) Nature , vol.362 , pp. 87-91
    • Eck, M.J.1    Shoelson, S.E.2    Harrison, S.C.3
  • 14
    • 0026605270 scopus 로고
    • A mutation in the catalytic domain of pp60v-src is responsible for the host-dependent and temperature-dependent phenotype of the Rous sarcoma virus muant tsLA33-1
    • Foster, R., and Martin, G.S. (1992). A mutation in the catalytic domain of pp60v-src is responsible for the host-dependent and temperature-dependent phenotype of the Rous sarcoma virus muant tsLA33-1. Virology 187, 145-155.
    • (1992) Virology , vol.187 , pp. 145-155
    • Foster, R.1    Martin, G.S.2
  • 16
    • 0025949757 scopus 로고
    • Effect of herbimycin-A on growth and pp60c-src activity in human colon tumor cell lines
    • Garcia, R., Parikh, N.U., Saya, H., and Gallick, G.E. (1991). Effect of herbimycin-A on growth and pp60c-src activity in human colon tumor cell lines. Oncogene 6, 1983-1989.
    • (1991) Oncogene , vol.6 , pp. 1983-1989
    • Garcia, R.1    Parikh, N.U.2    Saya, H.3    Gallick, G.E.4
  • 18
    • 0025010018 scopus 로고
    • Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells
    • Hirai, H., and Varmus, H.E. (1990b). Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells. Proc. Natl. Acad. Sci. USA 87, 8592-8596.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8592-8596
    • Hirai, H.1    Varmus, H.E.2
  • 19
    • 0028059879 scopus 로고
    • CSK suppression of Src involves movement of CSK to sites of Src activity
    • Howell, B.W., and Cooper, J.A. (1994). CSK suppression of Src involves movement of CSK to sites of Src activity. Mol. Cell. Biol. 14, 5402-5411.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5402-5411
    • Howell, B.W.1    Cooper, J.A.2
  • 20
    • 0023265819 scopus 로고
    • Adaptor plasmids simplify the insertion of foreign DNA into helper-independent retroviral vectors
    • Hughes, S.H., Greenhouse, J.J., Petropoulos, C.J., and Sutrave, P. (1987). Adaptor plasmids simplify the insertion of foreign DNA into helper-independent retroviral vectors. J. Virol. 61, 3004-3012.
    • (1987) J. Virol. , vol.61 , pp. 3004-3012
    • Hughes, S.H.1    Greenhouse, J.J.2    Petropoulos, C.J.3    Sutrave, P.4
  • 21
    • 0020596699 scopus 로고
    • Molecular events leading to fusiform morphological transformation by partial src deletion mutant of Rous sarcoma virus
    • Iswashita, S., Kitamura, N., and Yoshida, M. (1983). Molecular events leading to fusiform morphological transformation by partial src deletion mutant of Rous sarcoma virus. Virology 125, 419-431.
    • (1983) Virology , vol.125 , pp. 419-431
    • Iswashita, S.1    Kitamura, N.2    Yoshida, M.3
  • 23
    • 0022519437 scopus 로고
    • Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation
    • Kamps, M.P., Buss, J.E., and Sefton, B.M. (1986). Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation. Cell 45, 105-112.
    • (1986) Cell , vol.45 , pp. 105-112
    • Kamps, M.P.1    Buss, J.E.2    Sefton, B.M.3
  • 24
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan, K.B., Bibbins, K.B., Swedlow, J.R., Arnaud, M., Morgan, D.O., and Varmus, H.E. (1994). Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 23, 4745-4756.
    • (1994) EMBO J. , vol.23 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 25
    • 0023649672 scopus 로고
    • c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
    • c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49, 65-73.
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.E.1    Shalloway, D.2
  • 27
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-442.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-1442
    • Kunkel, T.A.1
  • 30
    • 0027214258 scopus 로고
    • The v-Src SH3 domain binds phosphatidylinositol 3′-kinase
    • Liu, X., Marengere, L.E.M., Koch, C.A., and Pawson, T. (1993a). The v-Src SH3 domain binds phosphatidylinositol 3′-kinase. Mol. Cell. Biol. 13, 5225-5232.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5225-5232
    • Liu, X.1    Marengere, L.E.M.2    Koch, C.A.3    Pawson, T.4
  • 31
    • 0026453585 scopus 로고
    • Identification of residues in GTPase-activating protein src homology-2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62
    • Marengere, L.E.M., and Pawson, T. (1992). Identification of residues in GTPase-activating protein src homology-2 domains that control binding to tyrosine phosphorylated growth factor receptors and p62. J. Biol. Chem. 267, 22779-22786.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22779-22786
    • Marengere, L.E.M.1    Pawson, T.2
  • 32
    • 0028721077 scopus 로고
    • Structure and function of SH2 domains
    • Marengere, L.E.M., and Pawson, T. (1994). Structure and function of SH2 domains. J. Cell Sci. Suppl. 18, 97-104.
    • (1994) J. Cell Sci. Suppl. , vol.18 , pp. 97-104
    • Marengere, L.E.M.1    Pawson, T.2
  • 33
    • 0026601293 scopus 로고
    • Point mutations in the v-abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo
    • Mayer, B.J., Jackson, P.K., Van Etten, R.A., and Baltimore, D. (1992). Point mutations in the v-abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol. Cell. Biol. 12, 609-618.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    Van Etten, R.A.3    Baltimore, D.4
  • 34
    • 0026767469 scopus 로고
    • She proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases
    • McGlade, J., Cheng, A., Pelicci, G., Pelicci, P.G., and Pawson, T. (1992). She proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc. Natl. Acad. Sci. USA 89, 8869-8873.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8869-8873
    • McGlade, J.1    Cheng, A.2    Pelicci, G.3    Pelicci, P.G.4    Pawson, T.5
  • 35
    • 0027261372 scopus 로고
    • Suppression of c-Src activity by C-terminal src kinase involves the c-Src SH2-domain and SH3-domain: Analysis with Saccharomyces cerevisiae
    • Murphy, S.M., Bergman, M., and Morgan, D.O. (1993). Suppression of c-Src activity by C-terminal src kinase involves the c-Src SH2-domain and SH3-domain: analysis with Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 5290-5300.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5290-5300
    • Murphy, S.M.1    Bergman, M.2    Morgan, D.O.3
  • 36
    • 0024554043 scopus 로고
    • Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein
    • Nemeth, S.P., Fox, L.G., DeMarco, M., and Brugge, J.S. (1989). Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein. Mol. Cell. Biol. 9, 1109-1119.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 1109-1119
    • Nemeth, S.P.1    Fox, L.G.2    Demarco, M.3    Brugge, J.S.4
  • 37
    • 0026605947 scopus 로고
    • Growth inhibition of human colorectal carcinoma cell lines by tumor necrosis factor-alpha correlates with reduced activity of pp60(c-src)
    • Novotnysmith, C.L., and Gallick, G.E. (1992). Growth inhibition of human colorectal carcinoma cell lines by tumor necrosis factor-alpha correlates with reduced activity of pp60(c-src). J. Immunother. 11, 159-168.
    • (1992) J. Immunother. , vol.11 , pp. 159-168
    • Novotnysmith, C.L.1    Gallick, G.E.2
  • 39
    • 0027219338 scopus 로고
    • Deletion of the SH3 domain of src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine
    • Okada, M., Howell, B.W., Broome, M.A., and Cooper, J.A. (1993). Deletion of the SH3 domain of src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine. J. Biol. Chem. 268, 18070-18075.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18070-18075
    • Okada, M.1    Howell, B.W.2    Broome, M.A.3    Cooper, J.A.4
  • 40
    • 0028173799 scopus 로고
    • Differential binding of pp60(c-src) and pp60(v-src) to cytoskeleton is mediated by SH2 and catalytic domains
    • Okamura, H., and Resh, M.D. (1994). Differential binding of pp60(c-src) and pp60(v-src) to cytoskeleton is mediated by SH2 and catalytic domains. Oncogene 9, 2293-2303.
    • (1994) Oncogene , vol.9 , pp. 2293-2303
    • Okamura, H.1    Resh, M.D.2
  • 43
    • 0024821548 scopus 로고
    • Genetics of src: Structure and functional organization of a protein tyrosine kinase
    • Parsons, J.T., and Weber, M.J. (1989). Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr. Top. Microbiol. Immunol. 147, 79-127.
    • (1989) Curr. Top. Microbiol. Immunol. , vol.147 , pp. 79-127
    • Parsons, J.T.1    Weber, M.J.2
  • 45
    • 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
  • 47
    • 0028260229 scopus 로고
    • Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src
    • Sabe, H., Hata, A., Okada, M., Nakagawa, H., and Hanafusa, H. (1994). Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc. Natl. Acad. Sci. USA 91, 3984-3988.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3984-3988
    • Sabe, H.1    Hata, A.2    Okada, M.3    Nakagawa, H.4    Hanafusa, H.5
  • 48
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai, R., Iwamatsu, A., Hirano, N., Ogawa, S., Tanaka, T., Mano, H., Yazaki, Y., and Hirai, H. (1994). A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13, 3748-3756.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 50
    • 0029081101 scopus 로고
    • SH2 domain structure and function
    • Schaffhausen, B. (1995). SH2 domain structure and function. Biochim. Biophys. Acta 1242, 61-75.
    • (1995) Biochim. Biophys. Acta , vol.1242 , pp. 61-75
    • Schaffhausen, B.1
  • 51
    • 0023016468 scopus 로고
    • From c-src to v-src, or the case of the missing C terminus
    • Sefton, B.M., and Hunter, T. (1986). From c-src to v-src, or the case of the missing C terminus. Cancer Surv. 5, 159-172.
    • (1986) Cancer Surv. , vol.5 , pp. 159-172
    • Sefton, B.M.1    Hunter, T.2
  • 52
    • 0026572318 scopus 로고
    • Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src
    • Seidel-Dugan, C., Meyer, B.E., Thomas, S.E., and Brugge, J.S. (1992). Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src. Mol. Cell. Biol. 12, 1835-1845.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1835-1845
    • Seidel-Dugan, C.1    Meyer, B.E.2    Thomas, S.E.3    Brugge, J.S.4
  • 54
    • 0022472990 scopus 로고
    • Requirement for c-ras proteins during viral oncogene transformation
    • Smith, M.R., DeGudicibus, S.J., and Stacey, D.W. (1986). Requirement for c-ras proteins during viral oncogene transformation. Nature 320, 540-543.
    • (1986) Nature , vol.320 , pp. 540-543
    • Smith, M.R.1    Degudicibus, S.J.2    Stacey, D.W.3
  • 56
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang, Z., et al. (1993). SH2 domains recognize specific phosphopeptide sequences. Cell 72, 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 57
    • 0026336517 scopus 로고
    • Dominant inhibitory Ras mutants demonstrate the requirement for Ras activity in the action of tyrosine kinase oncogenes
    • Stacey, D., Roudebush, M., Day, R., Mosser, S.D., Gibbs, J.B., and Feig, L.A. (1991). Dominant inhibitory Ras mutants demonstrate the requirement for Ras activity in the action of tyrosine kinase oncogenes. Oncogene 6, 2297-2304.
    • (1991) Oncogene , vol.6 , pp. 2297-2304
    • Stacey, D.1    Roudebush, M.2    Day, R.3    Mosser, S.D.4    Gibbs, J.B.5    Feig, L.A.6
  • 58
    • 0027182279 scopus 로고
    • Csk inhibition of c-src activity requires both the SH2 and SH3 domains of src
    • Superti-Furga, G., Fumagalli, S., Koegl, M., Courtneidge, S.A., and Draetta, G. (1993). Csk inhibition of c-src activity requires both the SH2 and SH3 domains of src. EMBO J. 12, 2625-2634.
    • (1993) EMBO J. , vol.12 , pp. 2625-2634
    • Superti-Furga, G.1    Fumagalli, S.2    Koegl, M.3    Courtneidge, S.A.4    Draetta, G.5
  • 59
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis
    • Taylor, S., and Shalloway, D. (1994). An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature 368, 867-871.
    • (1994) Nature , vol.368 , pp. 867-871
    • Taylor, S.1    Shalloway, D.2
  • 60
    • 0030033509 scopus 로고    scopus 로고
    • Reduced phosphotyrosine binding by the v-Src SH2 domain is compatible with wild type transformation
    • Tian, M., and Martin, G.S. (1996). Reduced phosphotyrosine binding by the v-Src SH2 domain is compatible with wild type transformation. Oncogene 11, 727-734.
    • (1996) Oncogene , vol.11 , pp. 727-734
    • Tian, M.1    Martin, G.S.2
  • 61
    • 0028984311 scopus 로고
    • v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and transformation-defective alleles of v-src
    • v-src autophosphorylation correlate with SHC-GRB2 complex formation in rat and chicken cells expressing host-range and transformation-defective alleles of v-src. Mol. Biol. Cell 6, 953-966.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 953-966
    • Verderame, M.F.1    Guan, J.-L.2    Ignatowski, K.M.W.3
  • 63
    • 0027954286 scopus 로고
    • Highly conserved amino acids in the SH2 and catalytic domains of v-src are altered in naturally occurring, transformation-defective alleles
    • Verderame, M.F., and Varmus, H.E. (1994). Highly conserved amino acids in the SH2 and catalytic domains of v-src are altered in naturally occurring, transformation-defective alleles. Oncogene 9, 175-182.
    • (1994) Oncogene , vol.9 , pp. 175-182
    • Verderame, M.F.1    Varmus, H.E.2
  • 64
    • 0026698924 scopus 로고
    • Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides
    • Waksman, G., et al. (1992). Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature 358, 646-653.
    • (1992) Nature , vol.358 , pp. 646-653
    • Waksman, G.1
  • 65
    • 0027409064 scopus 로고
    • Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain: Crystal structures of the complexed and peptide-free forms
    • Waksman, G., Shoelson, S.E., Pant, N., Cowburn, D., and Kurivan, J. (1993). Binding of a high affinity phosphotyrosyl peptide to the src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72, 779-790.
    • (1993) Cell , vol.72 , pp. 779-790
    • Waksman, G.1    Shoelson, S.E.2    Pant, N.3    Cowburn, D.4    Kurivan, J.5
  • 66
    • 0027944210 scopus 로고
    • Autophosphorylation is required for high kinase activity and efficient transforming ability of proteins encoded by host-range alleles of v-src
    • Woods, K.M., and Verderame, M.F. (1994). Autophosphorylation is required for high kinase activity and efficient transforming ability of proteins encoded by host-range alleles of v-src. J. Virol. 68, 7267-7274.
    • (1994) J. Virol. , vol.68 , pp. 7267-7274
    • Woods, K.M.1    Verderame, M.F.2
  • 67
    • 0023126096 scopus 로고
    • Genetic analysis of the form and function of the viral src oncogene product
    • Wyke, J.A., and Stoker, A.W. (1987). Genetic analysis of the form and function of the viral src oncogene product. Biochim. Biophys. Acta 907, 47-69.
    • (1987) Biochim. Biophys. Acta , vol.907 , pp. 47-69
    • Wyke, J.A.1    Stoker, A.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.