메뉴 건너뛰기




Volumn 324, Issue 4, 2004, Pages 1155-1164

Src protein-tyrosine kinase structure and regulation

Author keywords

Activation loop; ATP binding site; Csk binding protein; Hck; Membrane protein; Myristoylation; Non receptor protein tyrosine kinase; Oncogene; Phosphoserine; Phosphothreonine; Phosphotyrosine; Polyproline type II helix; Protein kinase A; Helix

Indexed keywords

AMINO ACID; EPIDERMAL GROWTH FACTOR RECEPTOR; PEPTIDE LIBRARY; PROTEIN SH2; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE P50(CSK);

EID: 13544256790     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.09.171     Document Type: Short Survey
Times cited : (459)

References (47)
  • 1
    • 0035374609 scopus 로고    scopus 로고
    • The hunting of the Src
    • G.S. Martin The hunting of the Src Nat. Rev. Mol. Cell Biol. 2 2001 467 775 An excellent summary of the discovery and elucidation of the properties of v-Src and Src
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 467-775
    • Martin, G.S.1
  • 2
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • M.T. Brown, and J.A. Cooper Regulation, substrates and functions of src Biochim. Biophys. Acta 1287 1996 121 149 A thorough review of the biochemical properties of Src
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 3
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • S.M. Thomas, and J.S. Brugge Cellular functions regulated by Src family kinases Annu. Rev. Cell Dev. Biol. 13 1997 513 609 A comprehensive review of the physiology and substrates of Src and Src-family kinases
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 5
    • 1542563409 scopus 로고    scopus 로고
    • Initial analysis and comparative analysis of the mouse genome
    • Mouse Genome Sequencing Consortium, Initial analysis and comparative analysis of the mouse genome, Nature 420 (2002) 520-562
    • (2002) Nature , vol.420 , pp. 520-562
  • 6
    • 0347445722 scopus 로고    scopus 로고
    • A genomic analysis of rat proteases and protease inhibitors
    • X.S. Puente, and C. López-Otín A genomic analysis of rat proteases and protease inhibitors Genome Res. 14 2004 609 622
    • (2004) Genome Res. , vol.14 , pp. 609-622
    • Puente, X.S.1    López-Otín, C.2
  • 7
    • 0037150728 scopus 로고    scopus 로고
    • Src in cancer: Deregulation and consequences for cell behaviour
    • M.C. Frame Src in cancer: deregulation and consequences for cell behaviour Biochim. Biophys. Acta 1602 2002 114 130
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 114-130
    • Frame, M.C.1
  • 8
    • 2942662100 scopus 로고    scopus 로고
    • Basis and importance of Src as a target in cancer
    • V.A. Levin Basis and importance of Src as a target in cancer Cancer Treat. Res. 119 2004 89 119
    • (2004) Cancer Treat. Res. , vol.119 , pp. 89-119
    • Levin, V.A.1
  • 10
    • 0034693877 scopus 로고    scopus 로고
    • Role of Src expression and activation in human cancer
    • R.B. Irby, and T.J. Yeatman Role of Src expression and activation in human cancer Oncogene 19 2000 5636 5642
    • (2000) Oncogene , vol.19 , pp. 5636-5642
    • Irby, R.B.1    Yeatman, T.J.2
  • 13
    • 0141788346 scopus 로고    scopus 로고
    • STI-571: An anticancer protein-tyrosine kinase inhibitor
    • R. Roskoski Jr. STI-571: an anticancer protein-tyrosine kinase inhibitor Biochem. Biophys. Res. Commun. 309 2003 709 717
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 709-717
    • Roskoski Jr., R.1
  • 14
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • G.B. Cohen, R. Ren, and D. Baltimore Modular binding domains in signal transduction proteins Cell 80 1995 237 248
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 15
    • 0028875162 scopus 로고
    • Recognition and specificity in protein-tyrosine kinase-mediated signaling
    • Z. Songyang, and L.C. Cantley Recognition and specificity in protein-tyrosine kinase-mediated signaling Trends Biochem. Sci. 20 1995 470 475
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 470-475
    • Songyang, Z.1    Cantley, L.C.2
  • 16
    • 2142758178 scopus 로고    scopus 로고
    • Structure and specificity of the SH2 domain
    • G. Waksman, and J. Kuriyan Structure and specificity of the SH2 domain Cell 116 2004 S45 S48
    • (2004) Cell , vol.116
    • Waksman, G.1    Kuriyan, J.2
  • 17
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPα
    • X.M. Zheng, R.J. Resnick, and D. Shalloway A phosphotyrosine displacement mechanism for activation of Src by PTPα EMBO J. 19 2000 964 978
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 19
    • 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 1987 65 73
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.E.1    Shalloway, D.2
  • 21
    • 0031035740 scopus 로고    scopus 로고
    • Association of Csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells
    • S. Zrihan-Licht, J. Lim, I. Keydar, M.X. Sliwkowski, J.E. Groopman, and H. Avraham Association of Csk-homologous kinase (CHK) (formerly MATK) with HER-2/ErbB-2 in breast cancer cells J. Biol. Chem. 272 1997 1856 1863
    • (1997) J. Biol. Chem. , vol.272 , pp. 1856-1863
    • Zrihan-Licht, S.1    Lim, J.2    Keydar, I.3    Sliwkowski, M.X.4    Groopman, J.E.5    Avraham, H.6
  • 22
    • 0034723419 scopus 로고    scopus 로고
    • Reciprocal regulation of Hck activity by phosphorylation of Tyr (527) and Tyr (416). Effect of introducing a high affinity intramolecular SH2 ligand
    • M. Porter, T. Schindler, J. Kuriyan, and W.T. Miller Reciprocal regulation of Hck activity by phosphorylation of Tyr (527) and Tyr (416). Effect of introducing a high affinity intramolecular SH2 ligand J. Biol. Chem. 275 2000 2721 2726
    • (2000) J. Biol. Chem. , vol.275 , pp. 2721-2726
    • Porter, M.1    Schindler, T.2    Kuriyan, J.3    Miller, W.T.4
  • 23
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • W. Xu, S.C. Harrison, and M.J. Eck Three-dimensional structure of the tyrosine kinase c-Src Nature 385 1997 595 602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 24
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • F. Sicheri, I. Moarefi, and J. Kuriyan Crystal structure of the Src family tyrosine kinase Hck Nature 385 1997 602 609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 25
  • 26
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • W. Xu, A. Doshi, M. Lei, M.J. Eck, and S.C. Harrison Crystal structures of c-Src reveal features of its autoinhibitory mechanism Mol. Cell 1999 629 638
    • (1999) Mol. Cell , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 27
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, V.A. Ashford, N.H. Xuong, S.S. Taylor, and J.M. Sowadski Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414 The first description of the tertiary structure of a protein kinase that serves as a model for all protein kinases
    • (1991) Science , vol.253 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.H.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 28
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • S.K. Hanks, A.M. Quinn, and T. Hunter The protein kinase family: conserved features and deduced phylogeny of the catalytic domains Science 241 1988 42 52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 29
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 30
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • S.C. Harrison Variation on an Src-like theme Cell 112 2003 737 740
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 31
    • 0036330594 scopus 로고    scopus 로고
    • Effect of autophosphorylation on the catalytic and regulatory properties of protein-tyrosine kinase Src
    • G. Sun, L. Ramdas, W. Wang, J. Vinci, J. McMurray, and R.J. Budde Effect of autophosphorylation on the catalytic and regulatory properties of protein-tyrosine kinase Src Arch. Biochem. Biophys. 397 2002 11 17
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 11-17
    • Sun, G.1    Ramdas, L.2    Wang, W.3    Vinci, J.4    McMurray, J.5    Budde, R.J.6
  • 32
    • 0032563970 scopus 로고    scopus 로고
    • Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation
    • G. Sun, A.K. Sharma, and R.J. Budde Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation Oncogene 17 1998 1587 1595
    • (1998) Oncogene , vol.17 , pp. 1587-1595
    • Sun, G.1    Sharma, A.K.2    Budde, R.J.3
  • 33
    • 0035916292 scopus 로고    scopus 로고
    • Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail
    • D. Wang, X.Y. Huang, and P.A. Cole Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail Biochemistry 40 2001 2004 2010
    • (2001) Biochemistry , vol.40 , pp. 2004-2010
    • Wang, D.1    Huang, X.Y.2    Cole, P.A.3
  • 34
    • 0034703099 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk
    • S. Takeuchi, Y. Takayama, A. Ogawa, K. Tamura, and M. Okada Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk J. Biol. Chem. 275 2000 29183 29186
    • (2000) J. Biol. Chem. , vol.275 , pp. 29183-29186
    • Takeuchi, S.1    Takayama, Y.2    Ogawa, A.3    Tamura, K.4    Okada, M.5
  • 36
    • 0038267169 scopus 로고    scopus 로고
    • Functions of the activation loop in Csk protein-tyrosine kinase
    • X. Lin, S. Lee, and G. Sun Functions of the activation loop in Csk protein-tyrosine kinase J. Biol. Chem. 278 2003 24072 24077
    • (2003) J. Biol. Chem. , vol.278 , pp. 24072-24077
    • Lin, X.1    Lee, S.2    Sun, G.3
  • 38
    • 0032488592 scopus 로고    scopus 로고
    • Peptide and protein phosphorylation by protein tyrosine kinase Csk: Insights into specificity and mechanism
    • D. Sondhi, W. Xu, Z. Songyang, M.J. Eck, and P.A. Cole Peptide and protein phosphorylation by protein tyrosine kinase Csk: insights into specificity and mechanism Biochemistry 37 1998 165 172
    • (1998) Biochemistry , vol.37 , pp. 165-172
    • Sondhi, D.1    Xu, W.2    Songyang, Z.3    Eck, M.J.4    Cole, P.A.5
  • 39
    • 0344736716 scopus 로고    scopus 로고
    • Determination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinase
    • S. Lee, X. Lin, N.H. Nam, K. Parang, and G. Sun Determination of the substrate-docking site of protein tyrosine kinase C-terminal Src kinase Proc. Natl. Acad. Sci. USA 100 2003 14707 14712
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14707-14712
    • Lee, S.1    Lin, X.2    Nam, N.H.3    Parang, K.4    Sun, G.5
  • 40
    • 2442701289 scopus 로고    scopus 로고
    • The ErbB/HER receptor protein-tyrosine kinases and cancer
    • R. Roskoski Jr. The ErbB/HER receptor protein-tyrosine kinases and cancer Biochem. Biophys. Res. Commun. 319 2004 1 11
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 1-11
    • Roskoski Jr., R.1
  • 41
    • 0017638132 scopus 로고
    • Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase
    • B.E. Kemp, D.J. Graves, E. Benjamini, and E.G. Krebs Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase J. Biol. Chem. 252 1977 4888 4894
    • (1977) J. Biol. Chem. , vol.252 , pp. 4888-4894
    • Kemp, B.E.1    Graves, D.J.2    Benjamini, E.3    Krebs, E.G.4
  • 42
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • E.H. Fischer, H. Charbonneau, and N.K. Tonks Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes Science 253 1991 401 406
    • (1991) Science , vol.253 , pp. 401-406
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, N.K.3
  • 43
    • 0017745268 scopus 로고
    • Identification of a transformation-specific antigen induced by an avian sarcoma virus
    • J.S. Brugge, and R.L. Erikson Identification of a transformation-specific antigen induced by an avian sarcoma virus Nature 269 1977 346 348
    • (1977) Nature , vol.269 , pp. 346-348
    • Brugge, J.S.1    Erikson, R.L.2
  • 44
    • 0005953097 scopus 로고
    • Protein kinase activity associated with the avian sarcoma virus src gene product
    • M.S. Collett, and R.L. Erikson Protein kinase activity associated with the avian sarcoma virus src gene product Proc. Natl. Acad. Sci. USA 75 1978 2021 2024
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2021-2024
    • Collett, M.S.1    Erikson, R.L.2
  • 45
    • 0018071189 scopus 로고
    • Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein
    • A.D. Levinson, H. Oppermann, L. Levintow, H.E. Varmus, and J.M. Bishop Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein Cell 15 1978 561 572
    • (1978) Cell , vol.15 , pp. 561-572
    • Levinson, A.D.1    Oppermann, H.2    Levintow, L.3    Varmus, H.E.4    Bishop, J.M.5
  • 46
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • T. Hunter, and B.M. Sefton Transforming gene product of Rous sarcoma virus phosphorylates tyrosine Proc. Natl. Acad. Sci. USA 77 1980 1311 1315
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 47
    • 0017250977 scopus 로고
    • DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA
    • D. Stehelin, H.E. Varmus, J.M. Bishop, and P.K. Vogt DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA Nature 260 1976 170 173
    • (1976) Nature , vol.260 , pp. 170-173
    • Stehelin, D.1    Varmus, H.E.2    Bishop, J.M.3    Vogt, P.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.