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Volumn 19, Issue 6, 2009, Pages 643-649

SH2 domains: modulators of nonreceptor tyrosine kinase activity

Author keywords

[No Author keywords available]

Indexed keywords

BRUTON TYROSINE KINASE; PROTEIN SH2; PROTEIN TYROSINE KINASE;

EID: 70649096122     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.10.001     Document Type: Review
Times cited : (89)

References (49)
  • 1
    • 0035575586 scopus 로고    scopus 로고
    • SH2 domains, interaction modules and cellular wiring
    • Pawson T., Gish G.D., and Nash P. SH2 domains, interaction modules and cellular wiring. Trends Cell Biol 11 (2001) 504-511
    • (2001) Trends Cell Biol , vol.11 , pp. 504-511
    • Pawson, T.1    Gish, G.D.2    Nash, P.3
  • 2
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu B.A., Jablonowski K., Raina M., Arce M., Pawson T., and Nash P.D. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol Cell 22 (2006) 851-868
    • (2006) Mol Cell , vol.22 , pp. 851-868
    • Liu, B.A.1    Jablonowski, K.2    Raina, M.3    Arce, M.4    Pawson, T.5    Nash, P.D.6
  • 3
    • 47249122274 scopus 로고    scopus 로고
    • Signaling properties of a non-metazoan Src kinase and the evolutionary history of Src negative regulation
    • Interesting study that describes the conservation of the SH2-kinase unit in different organisms and its development as a regulator of Src activity.
    • Li W., Young S.L., King N., and Miller W.T. Signaling properties of a non-metazoan Src kinase and the evolutionary history of Src negative regulation. J Biol Chem 283 (2008) 15491-15501. Interesting study that describes the conservation of the SH2-kinase unit in different organisms and its development as a regulator of Src activity.
    • (2008) J Biol Chem , vol.283 , pp. 15491-15501
    • Li, W.1    Young, S.L.2    King, N.3    Miller, W.T.4
  • 4
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer B.J., Hirai H., and Sakai R. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr Biol 5 (1995) 296-305
    • (1995) Curr Biol , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 5
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • Kuriyan J., and Eisenberg D. The origin of protein interactions and allostery in colocalization. Nature 450 (2007) 983-990
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 6
    • 0033025807 scopus 로고    scopus 로고
    • SH2 domains: from structure to energetics, a dual approach to the study of structure-function relationships
    • Grucza R.A., Bradshaw J.M., Futterer K., and Waksman G. SH2 domains: from structure to energetics, a dual approach to the study of structure-function relationships. Med Res Rev 19 (1999) 273-293
    • (1999) Med Res Rev , vol.19 , pp. 273-293
    • Grucza, R.A.1    Bradshaw, J.M.2    Futterer, K.3    Waksman, G.4
  • 7
    • 0033586726 scopus 로고    scopus 로고
    • Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics
    • Bradshaw J.M., and Waksman G. Calorimetric examination of high-affinity Src SH2 domain-tyrosyl phosphopeptide binding: dissection of the phosphopeptide sequence specificity and coupling energetics. Biochemistry 38 (1999) 5147-5154
    • (1999) Biochemistry , vol.38 , pp. 5147-5154
    • Bradshaw, J.M.1    Waksman, G.2
  • 8
    • 0033527682 scopus 로고    scopus 로고
    • Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase
    • Bradshaw J.M., Mitaxov V., and Waksman G. Investigation of phosphotyrosine recognition by the SH2 domain of the Src kinase. J Mol Biol 293 (1999) 971-985
    • (1999) J Mol Biol , vol.293 , pp. 971-985
    • Bradshaw, J.M.1    Mitaxov, V.2    Waksman, G.3
  • 11
    • 21444442110 scopus 로고    scopus 로고
    • Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins
    • Hu J., and Hubbard S.R. Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins. J Biol Chem 280 (2005) 18943-18949
    • (2005) J Biol Chem , vol.280 , pp. 18943-18949
    • Hu, J.1    Hubbard, S.R.2
  • 12
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W., Harrison S.C., and Eck M.J. 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
  • 13
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Identification of the mechanisms leads to Src inactivation by the N-terminal SH2 and SH3 domain.
    • Xu W., Doshi A., Lei M., Eck M.J., and Harrison S.C. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 3 (1999) 629-638. Identification of the mechanisms leads to Src inactivation by the N-terminal SH2 and SH3 domain.
    • (1999) Mol Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 14
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F., Moarefi I., and Kuriyan J. 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
  • 15
    • 0024829259 scopus 로고
    • A protein tyrosine kinase involved in regulation of pp60c-src function
    • Okada M., and Nakagawa H. A protein tyrosine kinase involved in regulation of pp60c-src function. J Biol Chem 264 (1989) 20886-20893
    • (1989) J Biol Chem , vol.264 , pp. 20886-20893
    • Okada, M.1    Nakagawa, H.2
  • 16
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young M.A., Gonfloni S., Superti-Furga G., Roux B., and Kuriyan J. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell 105 (2001) 115-126
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 18
    • 20444399897 scopus 로고    scopus 로고
    • The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation
    • This paper reports the active conformation of Src revealing a SH2 domain that forms no interaction with the active Scr kinase domain.
    • Cowan-Jacob S.W., Fendrich G., Manley P.W., Jahnke W., Fabbro D., Liebetanz J., and Meyer T. The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation. Structure 13 (2005) 861-871. This paper reports the active conformation of Src revealing a SH2 domain that forms no interaction with the active Scr kinase domain.
    • (2005) Structure , vol.13 , pp. 861-871
    • Cowan-Jacob, S.W.1    Fendrich, G.2    Manley, P.W.3    Jahnke, W.4    Fabbro, D.5    Liebetanz, J.6    Meyer, T.7
  • 19
    • 38549146411 scopus 로고    scopus 로고
    • Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering
    • Bernado P., Perez Y., Svergun D.I., and Pons M. Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering. J Mol Biol 376 (2008) 492-505
    • (2008) J Mol Biol , vol.376 , pp. 492-505
    • Bernado, P.1    Perez, Y.2    Svergun, D.I.3    Pons, M.4
  • 23
    • 34249105476 scopus 로고    scopus 로고
    • Structural basis for the inhibition of tyrosine kinase activity of ZAP-70
    • Report of the structure of the Zap70 inactive state suggests a mechanism of Zap70 activation by ICAM.
    • Deindl S., Kadlecek T.A., Brdicka T., Cao X., Weiss A., and Kuriyan J. Structural basis for the inhibition of tyrosine kinase activity of ZAP-70. Cell 129 (2007) 735-746. Report of the structure of the Zap70 inactive state suggests a mechanism of Zap70 activation by ICAM.
    • (2007) Cell , vol.129 , pp. 735-746
    • Deindl, S.1    Kadlecek, T.A.2    Brdicka, T.3    Cao, X.4    Weiss, A.5    Kuriyan, J.6
  • 24
    • 50149105176 scopus 로고    scopus 로고
    • Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling
    • Zhang Y., Oh H., Burton R.A., Burgner J.W., Geahlen R.L., and Post C.B. Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling. Proc Natl Acad Sci U S A 105 (2008) 11760-11765
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 11760-11765
    • Zhang, Y.1    Oh, H.2    Burton, R.A.3    Burgner, J.W.4    Geahlen, R.L.5    Post, C.B.6
  • 25
    • 0029936233 scopus 로고    scopus 로고
    • Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain
    • Xu B., and Miller W.T. Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain. Mol Cell Biochem 158 (1996) 57-63
    • (1996) Mol Cell Biochem , vol.158 , pp. 57-63
    • Xu, B.1    Miller, W.T.2
  • 26
    • 0033600568 scopus 로고    scopus 로고
    • Domain interactions in protein tyrosine kinase Csk
    • Sondhi D., and Cole P.A. Domain interactions in protein tyrosine kinase Csk. Biochemistry 38 (1999) 11147-11155
    • (1999) Biochemistry , vol.38 , pp. 11147-11155
    • Sondhi, D.1    Cole, P.A.2
  • 27
    • 0035900556 scopus 로고    scopus 로고
    • Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis
    • Shekhtman A., Ghose R., Wang D., Cole P.A., and Cowburn D. Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis. J Mol Biol 314 (2001) 129-138
    • (2001) J Mol Biol , vol.314 , pp. 129-138
    • Shekhtman, A.1    Ghose, R.2    Wang, D.3    Cole, P.A.4    Cowburn, D.5
  • 28
    • 0142138254 scopus 로고    scopus 로고
    • Protein tyrosine kinases Src and Csk: a tail's tale
    • Cole P.A., Shen K., Qiao Y., and Wang D. Protein tyrosine kinases Src and Csk: a tail's tale. Curr Opin Chem Biol 7 (2003) 580-585
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 580-585
    • Cole, P.A.1    Shen, K.2    Qiao, Y.3    Wang, D.4
  • 29
    • 0037177880 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal Src kinase, Csk
    • This paper reports the structure of active Csk revealing interactions of the kinase-SH2 linker region with the αC helix.
    • Ogawa A., Takayama Y., Sakai H., Chong K.T., Takeuchi S., Nakagawa A., Nada S., Okada M., and Tsukihara T. Structure of the carboxyl-terminal Src kinase, Csk. J Biol Chem 277 (2002) 14351-14354. This paper reports the structure of active Csk revealing interactions of the kinase-SH2 linker region with the αC helix.
    • (2002) J Biol Chem , vol.277 , pp. 14351-14354
    • Ogawa, A.1    Takayama, Y.2    Sakai, H.3    Chong, K.T.4    Takeuchi, S.5    Nakagawa, A.6    Nada, S.7    Okada, M.8    Tsukihara, T.9
  • 30
    • 0141737107 scopus 로고    scopus 로고
    • Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering
    • This study reports an interesting low-resolution model of an active full-length Tec family member.
    • Marquez J.A., Smith C.I., Petoukhov M.V., Lo Surdo P., Mattsson P.T., Knekt M., Westlund A., Scheffzek K., Saraste M., and Svergun D.I. Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering. EMBO J 22 (2003) 4616-4624. This study reports an interesting low-resolution model of an active full-length Tec family member.
    • (2003) EMBO J , vol.22 , pp. 4616-4624
    • Marquez, J.A.1    Smith, C.I.2    Petoukhov, M.V.3    Lo Surdo, P.4    Mattsson, P.T.5    Knekt, M.6    Westlund, A.7    Scheffzek, K.8    Saraste, M.9    Svergun, D.I.10
  • 31
    • 34248139038 scopus 로고    scopus 로고
    • The linker between SH2 and kinase domains positively regulates catalysis of the Tec family kinases
    • Joseph R.E., Min L., and Andreotti A.H. The linker between SH2 and kinase domains positively regulates catalysis of the Tec family kinases. Biochemistry 46 (2007) 5455-5462
    • (2007) Biochemistry , vol.46 , pp. 5455-5462
    • Joseph, R.E.1    Min, L.2    Andreotti, A.H.3
  • 32
    • 30344477956 scopus 로고    scopus 로고
    • Mutational analysis of the SH2-kinase linker region of Bruton's tyrosine kinase defines alternative modes of regulation for cytoplasmic tyrosine kinase families
    • Guo S., Wahl M.I., and Witte O.N. Mutational analysis of the SH2-kinase linker region of Bruton's tyrosine kinase defines alternative modes of regulation for cytoplasmic tyrosine kinase families. Int Immunol 18 (2006) 79-87
    • (2006) Int Immunol , vol.18 , pp. 79-87
    • Guo, S.1    Wahl, M.I.2    Witte, O.N.3
  • 33
    • 21844460518 scopus 로고    scopus 로고
    • The Jak1 SH2 domain does not fulfill a classical SH2 function in Jak/STAT signaling but plays a structural role for receptor interaction and up-regulation of receptor surface expression
    • Radtke S., Haan S., Jorissen A., Hermanns H.M., Diefenbach S., Smyczek T., Schmitz-Vandeleur H., Heinrich P.C., Behrmann I., and Haan C. The Jak1 SH2 domain does not fulfill a classical SH2 function in Jak/STAT signaling but plays a structural role for receptor interaction and up-regulation of receptor surface expression. J Biol Chem 280 (2005) 25760-25768
    • (2005) J Biol Chem , vol.280 , pp. 25760-25768
    • Radtke, S.1    Haan, S.2    Jorissen, A.3    Hermanns, H.M.4    Diefenbach, S.5    Smyczek, T.6    Schmitz-Vandeleur, H.7    Heinrich, P.C.8    Behrmann, I.9    Haan, C.10
  • 34
    • 33750522675 scopus 로고    scopus 로고
    • Jaks and cytokine receptors - an intimate relationship
    • Haan C., Kreis S., Margue C., and Behrmann I. Jaks and cytokine receptors - an intimate relationship. Biochem Pharmacol 72 (2006) 1538-1546
    • (2006) Biochem Pharmacol , vol.72 , pp. 1538-1546
    • Haan, C.1    Kreis, S.2    Margue, C.3    Behrmann, I.4
  • 36
    • 50249132542 scopus 로고    scopus 로고
    • Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation
    • First structural report of an active Fes kinase revealing the mechanisms by which the SH2 domain stabilizes the kinase active state. The paper provides also a comparison and mutational analysis with active Abl.
    • Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F., Salah E., Neudecker P., Kay L.E., Turk B.E., Superti-Furga G., et al. Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation. Cell 134 (2008) 793-803. First structural report of an active Fes kinase revealing the mechanisms by which the SH2 domain stabilizes the kinase active state. The paper provides also a comparison and mutational analysis with active Abl.
    • (2008) Cell , vol.134 , pp. 793-803
    • Filippakopoulos, P.1    Kofler, M.2    Hantschel, O.3    Gish, G.D.4    Grebien, F.5    Salah, E.6    Neudecker, P.7    Kay, L.E.8    Turk, B.E.9    Superti-Furga, G.10
  • 38
    • 0021173703 scopus 로고
    • Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis
    • This paper reports the SH2 domain for the first time as an activating motif in tyrosine kinases.
    • Stone J.C., Atkinson T., Smith M., and Pawson T. Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis. Cell 37 (1984) 549-558. This paper reports the SH2 domain for the first time as an activating motif in tyrosine kinases.
    • (1984) Cell , vol.37 , pp. 549-558
    • Stone, J.C.1    Atkinson, T.2    Smith, M.3    Pawson, T.4
  • 39
    • 0022977712 scopus 로고
    • A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps
    • Sadowski I., Stone J.C., and Pawson T. A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps. Mol Cell Biol 6 (1986) 4396-4408
    • (1986) Mol Cell Biol , vol.6 , pp. 4396-4408
    • Sadowski, I.1    Stone, J.C.2    Pawson, T.3
  • 40
    • 0021176463 scopus 로고
    • Mutagenesis of Fujinami sarcoma virus: evidence that tyrosine phosphorylation of P130gag-fps modulates its biological activity
    • Weinmaster G., Zoller M.J., Smith M., Hinze E., and Pawson T. Mutagenesis of Fujinami sarcoma virus: evidence that tyrosine phosphorylation of P130gag-fps modulates its biological activity. Cell 37 (1984) 559-568
    • (1984) Cell , vol.37 , pp. 559-568
    • Weinmaster, G.1    Zoller, M.J.2    Smith, M.3    Hinze, E.4    Pawson, T.5
  • 41
    • 0028641301 scopus 로고
    • Structural basis of SH2 domain mutations in X-linked agammaglobulinemia
    • Vihinen M., Nilsson L., and Smith C.I. Structural basis of SH2 domain mutations in X-linked agammaglobulinemia. Biochem Biophys Res Commun 205 (1994) 1270-1277
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 1270-1277
    • Vihinen, M.1    Nilsson, L.2    Smith, C.I.3
  • 43
    • 0033520933 scopus 로고    scopus 로고
    • Temperature-sensitive ZAP70 mutants degrading through a proteasome-independent pathway. Restoration of a kinase domain mutant by Cdc37
    • Matsuda S., Suzuki-Fujimoto T., Minowa A., Ueno H., Katamura K., and Koyasu S. Temperature-sensitive ZAP70 mutants degrading through a proteasome-independent pathway. Restoration of a kinase domain mutant by Cdc37. J Biol Chem 274 (1999) 34515-34518
    • (1999) J Biol Chem , vol.274 , pp. 34515-34518
    • Matsuda, S.1    Suzuki-Fujimoto, T.2    Minowa, A.3    Ueno, H.4    Katamura, K.5    Koyasu, S.6
  • 45
    • 46449121011 scopus 로고    scopus 로고
    • Genome wide analysis of pathogenic SH2 domain mutations
    • This paper provides a comprehensive overview of disease-causing mutations in Btk.
    • Lappalainen I., Thusberg J., Shen B., and Vihinen M. Genome wide analysis of pathogenic SH2 domain mutations. Proteins 72 (2008) 779-792. This paper provides a comprehensive overview of disease-causing mutations in Btk.
    • (2008) Proteins , vol.72 , pp. 779-792
    • Lappalainen, I.1    Thusberg, J.2    Shen, B.3    Vihinen, M.4
  • 48
    • 8944250665 scopus 로고    scopus 로고
    • Identification of Bruton's tyrosine kinase (Btk) gene mutations and characterization of the derived proteins in 35 X-linked agammaglobulinemia families: a nationwide study of Btk deficiency in Japan
    • Hashimoto S., Tsukada S., Matsushita M., Miyawaki T., Niida Y., Yachie A., Kobayashi S., Iwata T., Hayakawa H., Matsuoka H., et al. Identification of Bruton's tyrosine kinase (Btk) gene mutations and characterization of the derived proteins in 35 X-linked agammaglobulinemia families: a nationwide study of Btk deficiency in Japan. Blood 88 (1996) 561-573
    • (1996) Blood , vol.88 , pp. 561-573
    • Hashimoto, S.1    Tsukada, S.2    Matsushita, M.3    Miyawaki, T.4    Niida, Y.5    Yachie, A.6    Kobayashi, S.7    Iwata, T.8    Hayakawa, H.9    Matsuoka, H.10
  • 49
    • 66449085077 scopus 로고    scopus 로고
    • Girls homozygous for an IL-2-inducible T cell kinase mutation that leads to protein deficiency develop fatal EBV-associated lymphoproliferation
    • First identification of a disease-causing mutation in the SH2 domain of Itk.
    • Huck K., Feyen O., Niehues T., Ruschendorf F., Hubner N., Laws H.J., Telieps T., Knapp S., Wacker H.H., Meindl A., et al. Girls homozygous for an IL-2-inducible T cell kinase mutation that leads to protein deficiency develop fatal EBV-associated lymphoproliferation. J Clin Invest 119 (2009) 1350-1358. First identification of a disease-causing mutation in the SH2 domain of Itk.
    • (2009) J Clin Invest , vol.119 , pp. 1350-1358
    • Huck, K.1    Feyen, O.2    Niehues, T.3    Ruschendorf, F.4    Hubner, N.5    Laws, H.J.6    Telieps, T.7    Knapp, S.8    Wacker, H.H.9    Meindl, A.10


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