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Volumn 27, Issue 5, 2008, Pages 804-816

Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates

Author keywords

c Cbl; EGFR; Met; Reverse binding; Sprouty; TKB domain; X ray crystallography

Indexed keywords

ARGININE; ASPARAGINE; CBL PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; PHOSPHOTYROSINE; PROTEIN KINASE SYK; PROTEIN SH2; PROTEIN SPROUTY2; PROTEIN SPROUTY4; PROTEIN TYROSINE KINASE; SCATTER FACTOR RECEPTOR; SPROUTY PROTEIN; UNCLASSIFIED DRUG; GROWTH FACTOR RECEPTOR; MET PROTEIN, HUMAN; ONCOPROTEIN; PHOSPHOPEPTIDE; SIGNAL PEPTIDE; SPRY2 PROTEIN, HUMAN;

EID: 40949140084     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2008.18     Document Type: Article
Times cited : (59)

References (36)
  • 3
    • 34250361914 scopus 로고    scopus 로고
    • Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9
    • Ceccarelli DF, Blasutig IM, Goudreault M, Li Z, Ruston J, Pawson T, Sicheri F (2007) Non-canonical interaction of phosphoinositides with pleckstrin homology domains of Tiam1 and ArhGAP9. J Biol Chem 282: 13864-13874
    • (2007) J Biol Chem , vol.282 , pp. 13864-13874
    • Ceccarelli, D.F.1    Blasutig, I.M.2    Goudreault, M.3    Li, Z.4    Ruston, J.5    Pawson, T.6    Sicheri, F.7
  • 5
    • 2342558054 scopus 로고    scopus 로고
    • Structural basis for differential recognition of tyrosine- phosphorylated sites in the linker for activation of Tcells (LAT) by the adaptor Gads
    • Cho S, Velikovsky CA, Swaminathan CP, Houtman JC, Samelson LE, Mariuzza RA (2004) Structural basis for differential recognition of tyrosine- phosphorylated sites in the linker for activation of Tcells (LAT) by the adaptor Gads. EMBO J 23: 1441-1451
    • (2004) EMBO J , vol.23 , pp. 1441-1451
    • Cho, S.1    Velikovsky, C.A.2    Swaminathan, C.P.3    Houtman, J.C.4    Samelson, L.E.5    Mariuzza, R.A.6
  • 7
    • 0041355316 scopus 로고    scopus 로고
    • Bi-directional regulation of brown fat adipogenesis by the insulin receptor
    • Entingh AJ, Taniguchi CM, Kahn CR (2003) Bi-directional regulation of brown fat adipogenesis by the insulin receptor. J Biol Chem 278: 33377-33383
    • (2003) J Biol Chem , vol.278 , pp. 33377-33383
    • Entingh, A.J.1    Taniguchi, C.M.2    Kahn, C.R.3
  • 8
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng S, Chen JK, Yu H, Simon JA, Schreiber SL (1994) Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266: 1241-1247
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 10
    • 0141791276 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: An SH2 domain with altered specificity
    • Gunther UL, Weyrauch B, Zhang X, Schaffhausen B (2003) Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: an SH2 domain with altered specificity. Biochemistry 42: 11120-11127
    • (2003) Biochemistry , vol.42 , pp. 11120-11127
    • Gunther, U.L.1    Weyrauch, B.2    Zhang, X.3    Schaffhausen, B.4
  • 11
    • 0037452567 scopus 로고    scopus 로고
    • hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl
    • Hall AB, Jura N, DaSilva J, Jang YJ, Gong D, Bar-Sagi D (2003) hSpry2 is targeted to the ubiquitin-dependent proteasome pathway by c-Cbl. Curr Biol 13: 308-314
    • (2003) Curr Biol , vol.13 , pp. 308-314
    • Hall, A.B.1    Jura, N.2    DaSilva, J.3    Jang, Y.J.4    Gong, D.5    Bar-Sagi, D.6
  • 12
    • 21444442110 scopus 로고    scopus 로고
    • Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins
    • Hu J, Hubbard SR (2005) Structural characterization of a novel Cbl phosphotyrosine recognition motif in the APS family of adapter proteins. J Biol Chem 280: 18943-18949
    • (2005) J Biol Chem , vol.280 , pp. 18943-18949
    • Hu, J.1    Hubbard, S.R.2
  • 13
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC (1999) The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 286: 309-312
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47 (Part 2): 110-119
    • (1991) Acta Crystallogr A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 15
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacAuthur MW, Moss DS, Thornton JM (1993) Procheck: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacAuthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 17
    • 33745185987 scopus 로고    scopus 로고
    • The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling
    • Liu BA, Jablonowski K, Raina M, Arce M, Pawson T, Nash PD (2006) The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Mol Cell 22: 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
  • 18
    • 0036098461 scopus 로고    scopus 로고
    • APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes
    • Liu J, Kimura A, Baumann CA, Saltiel AR (2002) APS facilitates c-Cbl tyrosine phosphorylation and GLUT4 translocation in response to insulin in 3T3-L1 adipocytes. Mol Cell Biol 22: 3599-3609
    • (2002) Mol Cell Biol , vol.22 , pp. 3599-3609
    • Liu, J.1    Kimura, A.2    Baumann, C.A.3    Saltiel, A.R.4
  • 19
    • 14444276991 scopus 로고    scopus 로고
    • The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70
    • Lupher Jr ML, Songyang Z, Shoelson SE, Cantley LC, Band H (1997) The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70. J Biol Chem 272: 33140-33144
    • (1997) J Biol Chem , vol.272 , pp. 33140-33144
    • Lupher Jr, M.L.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 20
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • Machida K, Mayer BJ (2005) The SH2 domain: versatile signaling module and pharmaceutical target. Biochim Biophys Acta 1747: 1-25
    • (2005) Biochim Biophys Acta , vol.1747 , pp. 1-25
    • Machida, K.1    Mayer, B.J.2
  • 21
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
    • Meng W, Sawasdikosol S, Burakoff SJ, Eck MJ (1999) Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 398: 84-90
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276 (Part A): 307-326
    • (1997) Methods Enzymol , vol.276 , Issue.PART A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0037534097 scopus 로고    scopus 로고
    • c-Cbl is a critical modulator of the Ron tyrosine kinase receptor
    • Penengo L, Rubin C, Yarden Y, Gaudino G (2003) c-Cbl is a critical modulator of the Ron tyrosine kinase receptor. Oncogene 22: 3669-3679
    • (2003) Oncogene , vol.22 , pp. 3669-3679
    • Penengo, L.1    Rubin, C.2    Yarden, Y.3    Gaudino, G.4
  • 24
    • 0035930341 scopus 로고    scopus 로고
    • Mutation of the c-Cbl TKB domain binding site on the Met receptor tyrosine kinase converts it into a transforming protein
    • Peschard P, Fournier TM, Lamorte L, Naujokas MA, Band H, Langdon WY, Park M (2001) Mutation of the c-Cbl TKB domain binding site on the Met receptor tyrosine kinase converts it into a transforming protein. Mol Cell 8: 995-1004
    • (2001) Mol Cell , vol.8 , pp. 995-1004
    • Peschard, P.1    Fournier, T.M.2    Lamorte, L.3    Naujokas, M.A.4    Band, H.5    Langdon, W.Y.6    Park, M.7
  • 25
    • 3142761786 scopus 로고    scopus 로고
    • A conserved DpYR motif in the juxtamembrane domain of the Met receptor family forms an atypical c-Cbl/Cbl-b tyrosine kinase binding domain binding site required for suppression of oncogenic activation
    • Peschard P, Ishiyama N, Lin T, Lipkowitz S, Park M (2004) A conserved DpYR motif in the juxtamembrane domain of the Met receptor family forms an atypical c-Cbl/Cbl-b tyrosine kinase binding domain binding site required for suppression of oncogenic activation. J Biol Chem 279: 29565-29571
    • (2004) J Biol Chem , vol.279 , pp. 29565-29571
    • Peschard, P.1    Ishiyama, N.2    Lin, T.3    Lipkowitz, S.4    Park, M.5
  • 26
    • 0038386452 scopus 로고    scopus 로고
    • Escape from Cbl-mediated downregulation: A recurrent theme for oncogenic deregulation of receptor tyrosine kinases
    • Peschard P, Park M (2003) Escape from Cbl-mediated downregulation: a recurrent theme for oncogenic deregulation of receptor tyrosine kinases. Cancer Cell 3: 519-523
    • (2003) Cancer Cell , vol.3 , pp. 519-523
    • Peschard, P.1    Park, M.2
  • 27
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • Reverter D, Lima CD (2005) Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435: 687-692
    • (2005) Nature , vol.435 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 28
    • 0242684548 scopus 로고    scopus 로고
    • Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops
    • Rubin C, Litvak V, Medvedovsky H, Zwang Y, Lev S, Yarden Y (2003) Sprouty fine-tunes EGF signaling through interlinked positive and negative feedback loops. Curr Biol 13: 297-307
    • (2003) Curr Biol , vol.13 , pp. 297-307
    • Rubin, C.1    Litvak, V.2    Medvedovsky, H.3    Zwang, Y.4    Lev, S.5    Yarden, Y.6
  • 29
    • 28844490931 scopus 로고    scopus 로고
    • The Cbl interactome and its functions
    • Schmidt MH, Dikic I (2005) The Cbl interactome and its functions. Nat Rev Mol Cell Biol 6: 907-919
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 907-919
    • Schmidt, M.H.1    Dikic, I.2
  • 30
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: A reversal of the bound orientation
    • Song J, Zhang Z, Hu W, Chen Y (2005) Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J Biol Chem 280: 40122-40129
    • (2005) J Biol Chem , vol.280 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 32
    • 27444445613 scopus 로고    scopus 로고
    • c-Cbl and Cbl-b ubiquitin ligases: Substrate diversity and the negative regulation of signalling responses
    • Thien CB, Langdon WY (2005) c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signalling responses. Biochem J 391 (Part 2): 153-166
    • (2005) Biochem J , vol.391 , Issue.PART 2 , pp. 153-166
    • Thien, C.B.1    Langdon, W.Y.2
  • 33
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A (1997) MOLREP: an automated program for molecular replacement. J Appl Cryst 30: 1022-1025
    • (1997) J Appl Cryst , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 34
    • 0037119950 scopus 로고    scopus 로고
    • Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling
    • Wong ES, Fong CW, Lim J, Yusoff P, Low BC, Langdon WY, Guy GR (2002) Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling. EMBO J 21: 4796-4808
    • (2002) EMBO J , vol.21 , pp. 4796-4808
    • Wong, E.S.1    Fong, C.W.2    Lim, J.3    Yusoff, P.4    Low, B.C.5    Langdon, W.Y.6    Guy, G.R.7
  • 35
    • 0035937167 scopus 로고    scopus 로고
    • Evidence for direct interaction between Sprouty and Cbl
    • Wong ES, Lim J, Low BC, Chen Q, Guy GR (2001) Evidence for direct interaction between Sprouty and Cbl. J Biol Chem 276: 5866-5875
    • (2001) J Biol Chem , vol.276 , pp. 5866-5875
    • Wong, E.S.1    Lim, J.2    Low, B.C.3    Chen, Q.4    Guy, G.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.