메뉴 건너뛰기




Volumn 33, Issue 11, 2013, Pages 2188-2201

Structural basis for activation of ZAP-70 by phosphorylation of the SH2-kinase linker

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE LCK; PROTEIN KINASE SYK; PROTEIN KINASE ZAP 70; PROTEIN SH2; TYROSINE;

EID: 84878999914     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01637-12     Document Type: Article
Times cited : (82)

References (44)
  • 4
    • 0032498231 scopus 로고    scopus 로고
    • LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE. 1998. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92:83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 7
    • 37049019860 scopus 로고    scopus 로고
    • Opposing functions of the T cell receptor kinase ZAP-70 in immunity and tolerance differentially titrate in response to nucleotide substitutions
    • Siggs OM, Miosge LA, Yates AL, Kucharska EM, Sheahan D, Brdicka T, Weiss A, Liston A, Goodnow CC. 2007. Opposing functions of the T cell receptor kinase ZAP-70 in immunity and tolerance differentially titrate in response to nucleotide substitutions. Immunity 27:912-926.
    • (2007) Immunity , vol.27 , pp. 912-926
    • Siggs, O.M.1    Miosge, L.A.2    Yates, A.L.3    Kucharska, E.M.4    Sheahan, D.5    Brdicka, T.6    Weiss, A.7    Liston, A.8    Goodnow, C.C.9
  • 8
    • 70449721003 scopus 로고    scopus 로고
    • A hypomorphic allele of ZAP-70 reveals a distinct thymic threshold for autoimmune disease versus autoimmune reactivity
    • Hsu LY, Tan YX, Xiao Z, Malissen M, Weiss A. 2009. A hypomorphic allele of ZAP-70 reveals a distinct thymic threshold for autoimmune disease versus autoimmune reactivity. J. Exp. Med. 206:2527-2541.
    • (2009) J. Exp. Med. , vol.206 , pp. 2527-2541
    • Hsu, L.Y.1    Tan, Y.X.2    Xiao, Z.3    Malissen, M.4    Weiss, A.5
  • 9
    • 0029347999 scopus 로고
    • The Syk/ZAP-70 protein tyrosine kinase connection to antigen receptor signalling processes
    • Van Oers NS, Weiss A. 1995. The Syk/ZAP-70 protein tyrosine kinase connection to antigen receptor signalling processes. Semin. Immunol. 7:227-236.
    • (1995) Semin. Immunol. , vol.7 , pp. 227-236
    • Van Oers, N.S.1    Weiss, A.2
  • 10
    • 0028292001 scopus 로고
    • Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase
    • Elder ME, Lin D, Clever J, Chan AC, Hope TJ, Weiss A, Parslow TG. 1994. Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase. Science 264:1596-1599.
    • (1994) Science , vol.264 , pp. 1596-1599
    • Elder, M.E.1    Lin, D.2    Clever, J.3    Chan, A.C.4    Hope, T.J.5    Weiss, A.6    Parslow, T.G.7
  • 11
    • 0035159584 scopus 로고    scopus 로고
    • Distinct T cell developmental consequences in humans and mice expressing identical mutations in the DLAARN motif of ZAP-70
    • Elder ME, Skoda-Smith S, Kadlecek TA, Wang F, Wu J, Weiss A. 2001. Distinct T cell developmental consequences in humans and mice expressing identical mutations in the DLAARN motif of ZAP-70. J. Immunol. 166:656-661.
    • (2001) J. Immunol. , vol.166 , pp. 656-661
    • Elder, M.E.1    Skoda-Smith, S.2    Kadlecek, T.A.3    Wang, F.4    Wu, J.5    Weiss, A.6
  • 12
    • 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, Koyasu S. 1999. Temperature-sensitive ZAP70 mutants degrading through a proteasome-independent pathway. Restoration of a kinase domain mutant by Cdc37. J. Biol. Chem. 274:34515-34518.
    • (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
  • 14
    • 0032555744 scopus 로고    scopus 로고
    • Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide
    • Futterer K, Wong J, Grucza RA, Chan AC, Waksman G. 1998. Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J. Mol. Biol. 281:523-537.
    • (1998) J. Mol. Biol. , vol.281 , pp. 523-537
    • Futterer, K.1    Wong, J.2    Grucza, R.A.3    Chan, A.C.4    Waksman, G.5
  • 15
    • 0037016021 scopus 로고    scopus 로고
    • Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem
    • Folmer RH, Geschwindner S, Xue Y. 2002. Crystal structure and NMR studies of the apo SH2 domains of ZAP-70: two bikes rather than a tandem. Biochemistry 41:14176-14184.
    • (2002) Biochemistry , vol.41 , pp. 14176-14184
    • Folmer, R.H.1    Geschwindner, S.2    Xue, Y.3
  • 16
    • 0040799939 scopus 로고    scopus 로고
    • Thermodynamic study of the binding of the tandem-SH2 domain of the Syk kinase to a dually phosphorylated ITAM peptide: evidence for two conformers
    • Grucza RA, Futterer K, Chan AC, Waksman G. 1999. Thermodynamic study of the binding of the tandem-SH2 domain of the Syk kinase to a dually phosphorylated ITAM peptide: evidence for two conformers. Biochemistry 38:5024-5033.
    • (1999) Biochemistry , vol.38 , pp. 5024-5033
    • Grucza, R.A.1    Futterer, K.2    Chan, A.C.3    Waksman, G.4
  • 17
    • 34249105476 scopus 로고    scopus 로고
    • Structural basis for the inhibition of tyrosine kinase activity of ZAP-70
    • Deindl S, Kadlecek TA, Brdicka T, Cao X, Weiss A, Kuriyan J. 2007. Structural basis for the inhibition of tyrosine kinase activity of ZAP-70. Cell 129:735-746.
    • (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
  • 18
    • 73949155450 scopus 로고    scopus 로고
    • Stability of an autoinhibitory interface in the structure of the tyrosine kinase ZAP-70 impacts T cell receptor response
    • Deindl S, Kadlecek TA, Cao X, Kuriyan J, Weiss A. 2009. Stability of an autoinhibitory interface in the structure of the tyrosine kinase ZAP-70 impacts T cell receptor response. Proc. Natl. Acad. Sci. U. S. A. 106:20699-20704.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20699-20704
    • Deindl, S.1    Kadlecek, T.A.2    Cao, X.3    Kuriyan, J.4    Weiss, A.5
  • 19
    • 20344406482 scopus 로고    scopus 로고
    • Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases
    • Brdicka T, Kadlecek TA, Roose JP, Pastuszak AW, Weiss A. 2005. Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases. Mol. Cell. Biol. 25:4924-4933.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4924-4933
    • Brdicka, T.1    Kadlecek, T.A.2    Roose, J.P.3    Pastuszak, A.W.4    Weiss, A.5
  • 20
    • 0035920572 scopus 로고    scopus 로고
    • Requirement for tyrosine residues 315 and 319 within zeta chain-associated protein 70 for T cell development
    • Gong Q, Jin X, Akk AM, Foger N, White M, Gong G, Bubeck Wardenburg J, Chan AC. 2001. Requirement for tyrosine residues 315 and 319 within zeta chain-associated protein 70 for T cell development. J. Exp. Med. 194:507-518.
    • (2001) J. Exp. Med. , vol.194 , pp. 507-518
    • Gong, Q.1    Jin, X.2    Akk, A.M.3    Foger, N.4    White, M.5    Gong, G.6    Bubeck Wardenburg, J.7    Chan, A.C.8
  • 23
    • 0030914118 scopus 로고    scopus 로고
    • The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction
    • Wu J, Zhao Q, Kurosaki T, Weiss A. 1997. The Vav binding site (Y315) in ZAP-70 is critical for antigen receptor-mediated signal transduction. J. Exp. Med. 185:1877-1882.
    • (1997) J. Exp. Med. , vol.185 , pp. 1877-1882
    • Wu, J.1    Zhao, Q.2    Kurosaki, T.3    Weiss, A.4
  • 27
    • 84892901456 scopus 로고    scopus 로고
    • Processing diffraction data with Mosflm. Evolving Methods Macromol
    • Leslie AGW, Powell HR. 2007. Processing diffraction data with Mosflm. Evolving Methods Macromol. Crystallogr. 245:11.
    • (2007) Crystallogr , vol.245 , pp. 11
    • Leslie, A.G.W.1    Powell, H.R.2
  • 29
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn MD, Murshudov GN, Papiz MZ. 2003. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374: 300-321.
    • (2003) Methods Enzymol. , vol.374 , pp. 300-321
    • Winn, M.D.1    Murshudov, G.N.2    Papiz, M.Z.3
  • 32
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E. 2008. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4:435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 36
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: a parallel linear constraint solver for molecular simulation
    • Hess B. 2008. P-LINCS: a parallel linear constraint solver for molecular simulation. J. Chem. Theory Comput. 4:116-122.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 116-122
    • Hess, B.1
  • 37
    • 0019707626 scopus 로고
    • Polymorphic transitions in singlecrystals-a new molecular-dynamics method
    • Parrinello M, Rahman A. 1981. Polymorphic transitions in singlecrystals-a new molecular-dynamics method. J. Appl. Phys. 52:7182-7190.
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 38
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F, Moarefi I, Kuriyan J. 1997. Crystal structure of the Src family tyrosine kinase Hck. Nature 385:602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 39
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W, Harrison SC, Eck MJ. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 41
    • 61349122046 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent in vitro reconstitution of recombinant LAT-nucleated multiprotein signalling complexes on liposomes
    • Sangani D, Venien-Bryan C, Harder T. 2009. Phosphotyrosine-dependent in vitro reconstitution of recombinant LAT-nucleated multiprotein signalling complexes on liposomes. Mol. Membr. Biol. 26:159-170.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 159-170
    • Sangani, D.1    Venien-Bryan, C.2    Harder, T.3
  • 43
    • 33847659183 scopus 로고    scopus 로고
    • c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty
    • Seeliger MA, Nagar B, Frank F, Cao X, Henderson MN, Kuriyan J. 2007. c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty. Structure 15:299-311.
    • (2007) Structure , vol.15 , pp. 299-311
    • Seeliger, M.A.1    Nagar, B.2    Frank, F.3    Cao, X.4    Henderson, M.N.5    Kuriyan, J.6
  • 44
    • 0029866039 scopus 로고    scopus 로고
    • Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes.
    • van Oers NS, Killeen N, Weiss A. 1996. Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. J. Exp. Med. 183:1053-1062.
    • (1996) J. Exp. Med. , vol.183 , pp. 1053-1062
    • van Oers, N.S.1    Killeen, N.2    Weiss, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.