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Volumn 277, Issue 21, 2010, Pages 4356-4369

Docking proteins

Author keywords

Dok; DOS; FRS2; Gab; IRS; Protein modules; Protein phosphorylation; SH2; Signal transduction; Tyrosine kinase

Indexed keywords

DOCKING PROTEIN; DOWNSTREAM OF TYROSINE KINASE; FIBROBLAST GROWTH FACTOR RECEPTOR SUBSTRATE 2; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2 ASSOCIATED BINDER; INSULIN RECEPTOR SUBSTRATE; UNCLASSIFIED DRUG; GRB2 PROTEIN, HUMAN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE;

EID: 79952111041     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07865.x     Document Type: Short Survey
Times cited : (38)

References (142)
  • 1
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103, 211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 2
    • 70350376377 scopus 로고    scopus 로고
    • Regulation of lymphocyte development and activation by the LAT family of adapter proteins
    • Fuller DM & Zhang W (2009) Regulation of lymphocyte development and activation by the LAT family of adapter proteins. Immunol Rev 232, 72-83.
    • (2009) Immunol Rev , vol.232 , pp. 72-83
    • Fuller, D.M.1    Zhang, W.2
  • 3
    • 0032577051 scopus 로고    scopus 로고
    • The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: Its role in cell growth and disease
    • Hunter T (1998) The Croonian Lecture 1997. The phosphorylation of proteins on tyrosine: its role in cell growth and disease. Phil Trans R Soc Lond B 353, 583-605.
    • (1998) Phil Trans R Soc Lond B , vol.353 , pp. 583-605
    • Hunter, T.1
  • 4
    • 33646557326 scopus 로고    scopus 로고
    • P130Cas: A versatile scaffold in signaling networks
    • DOI 10.1016/j.tcb.2006.03.003, PII S0962892406000833
    • Defilippi P, Di Stefano P & Cabodi S (2006) p130Cas: a versatile scaffold in signaling networks. Trends Cell Biol 16, 257-263. (Pubitemid 43728873)
    • (2006) Trends in Cell Biology , vol.16 , Issue.5 , pp. 257-263
    • Defilippi, P.1    Di, S.P.2    Cabodi, S.3
  • 5
    • 33244490746 scopus 로고    scopus 로고
    • SLP76 and SLP65: Complex regulation of signalling in lymphocytes and beyond
    • DOI 10.1038/nri1750, PII N1750
    • Koretzky GA, Abtahian F & Silverman MA (2006) SLP76 and SLP65: complex regulation of signalling in lymphocytes and beyond. Nat Rev Immunol 6, 67-78. (Pubitemid 43279754)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.1 , pp. 67-78
    • Koretzky, G.A.1    Abtahian, F.2    Silverman, M.A.3
  • 6
    • 44449108785 scopus 로고    scopus 로고
    • Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins
    • Gotoh N (2008) Regulation of growth factor signaling by FRS2 family docking/scaffold adaptor proteins. Cancer Sci 99, 1319-1325.
    • (2008) Cancer Sci , vol.99 , pp. 1319-1325
    • Gotoh, N.1
  • 7
    • 77955599451 scopus 로고    scopus 로고
    • Function, regulation and pathological roles of the Gab/DOS docking proteins
    • Wohrle FU, Daly RJ & Brummer T (2009) Function, regulation and pathological roles of the Gab/DOS docking proteins. Cell Commun Signal 7, 22.
    • (2009) Cell Commun Signal , vol.7 , pp. 22
    • Wohrle, F.U.1    Daly, R.J.2    Brummer, T.3
  • 8
    • 0042030799 scopus 로고    scopus 로고
    • Grb2-independent recruitment of Gab1 requires the C-terminal lobe and structural integrity of the met receptor kinase domain
    • DOI 10.1074/jbc.M302675200
    • Lock LS, Frigault MM, Saucier C & Park M (2003) Grb2-independent recruitment of Gab1 requires the C-terminal lobe and structural integrity of the Met receptor kinase domain. J Biol Chem 278, 30083-30090. (Pubitemid 36962400)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 30083-30090
    • Lock, L.S.1    Frigault, M.M.2    Saucier, C.3    Park, M.4
  • 9
    • 0033959896 scopus 로고    scopus 로고
    • A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling
    • DOI 10.1128/MCB.20.4.1448-1459.2000
    • Rodrigues GA, Falasca M, Zhang Z, Ong SH & Schlessinger J (2000) A novel positive feedback loop mediated by the docking protein Gab1 and phosphatidylinositol 3-kinase in epidermal growth factor receptor signaling. Mol Cell Biol 20, 1448-1459. (Pubitemid 30069264)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.4 , pp. 1448-1459
    • Rodrigues, G.A.1    Falasca, M.2    Zhang, Z.3    Ong, S.H.4    Schlessinger, J.5
  • 10
    • 0034613198 scopus 로고    scopus 로고
    • Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases
    • Lock LS, Royal I, Naujokas MA & Park M (2000) Identification of an atypical Grb2 carboxyl-terminal SH3 domain binding site in Gab docking proteins reveals Grb2-dependent and -independent recruitment of Gab1 to receptor tyrosine kinases. J Biol Chem 275, 31536-31545.
    • (2000) J Biol Chem , vol.275 , pp. 31536-31545
    • Lock, L.S.1    Royal, I.2    Naujokas, M.A.3    Park, M.4
  • 12
    • 76349118326 scopus 로고    scopus 로고
    • Differential phosphorylation of the docking protein Gab1 by c-Src and the hepatocyte growth factor receptor regulates different aspects of cell functions
    • Chan PC, Sudhakar JN, Lai CC & Chen HC (2010) Differential phosphorylation of the docking protein Gab1 by c-Src and the hepatocyte growth factor receptor regulates different aspects of cell functions. Oncogene 29, 698-710.
    • (2010) Oncogene , vol.29 , pp. 698-710
    • Chan, P.C.1    Sudhakar, J.N.2    Lai, C.C.3    Chen, H.C.4
  • 13
    • 0034607968 scopus 로고    scopus 로고
    • Requirement of SHP2 binding to Grb2-associated binder-1 for mitogen- Activated protein kinase activation in response to lysophosphatidic acid and epidermal growth factor
    • DOI 10.1074/jbc.275.18.13842
    • Cunnick JM, Dorsey JF, Munoz-Antonia T, Mei L & Wu J (2000) Requirement of SHP2 binding to Grb2-associated binder-1 for mitogen-activated protein kinase activation in response to lysophosphatidic acid and epidermal growth factor. J Biol Chem 275, 13842-13848. (Pubitemid 30257458)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.18 , pp. 13842-13848
    • Cunnick, J.M.1    Dorsey, J.F.2    Munoz-Antonia, T.3    Mei, L.4    Wu, J.5
  • 14
    • 0033761488 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP-2 is required for sustained activation of extracellular signal-regulated kinase and epithelial morphogenesis downstream from the met receptor tyrosine kinase
    • Maroun CR, Naujokas MA, Holgado-Madruga M, Wong AJ & Park M (2000) The tyrosine phosphatase SHP-2 is required for sustained activation of extracellular signal-regulated kinase and epithelial morphogenesis downstream from the met receptor tyrosine kinase. Mol Cell Biol 20, 8513-8525.
    • (2000) Mol Cell Biol , vol.20 , pp. 8513-8525
    • Maroun, C.R.1    Naujokas, M.A.2    Holgado-Madruga, M.3    Wong, A.J.4    Park, M.5
  • 16
    • 26844514477 scopus 로고    scopus 로고
    • Participation of both Gab1 and Gab2 in the activation of the ERK/MAPK pathway by epidermal growth factor
    • DOI 10.1042/BJ20050229
    • Meng S, Chen Z, Munoz-Antonia T & Wu J (2005) Participation of both Gab1 and Gab2 in the activation of the ERK/MAPK pathway by epidermal growth factor. Biochem J 391, 143-151. (Pubitemid 41445485)
    • (2005) Biochemical Journal , vol.391 , Issue.1 , pp. 143-151
    • Meng, S.1    Chen, Z.2    Munoz-Antonia, T.3    Wu, J.4
  • 17
    • 33644850529 scopus 로고    scopus 로고
    • Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein
    • DOI 10.1074/jbc.M509567200
    • Brummer T, Schramek D, Hayes VM, Bennett HL, Caldon CE, Musgrove EA & Daly RJ (2006) Increased proliferation and altered growth factor dependence of human mammary epithelial cells overexpressing the Gab2 docking protein. J Biol Chem 281, 626-637. (Pubitemid 43671226)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 626-637
    • Brummer, T.1    Schramek, D.2    Hayes, V.M.3    Bennett, H.L.4    Caldon, C.E.5    Musgrove, E.A.6    Daly, R.J.7
  • 18
    • 33749376770 scopus 로고    scopus 로고
    • The scaffolding adapter Gab2, via Shp-2, regulates Kit-evoked mast cell proliferation by activating the Rac/JNK pathway
    • DOI 10.1074/jbc.M603742200
    • Yu M, Luo J, Yang W, Wang Y, Mizuki M, Kanakura Y, Besmer P, Neel BG & Gu H (2006) The scaffolding adapter Gab2, via Shp-2, regulates kit-evoked mast cell proliferation by activating the Rac/JNK pathway. J Biol Chem 281, 28615-28626. (Pubitemid 44507004)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28615-28626
    • Yu, M.1    Luo, J.2    Yang, W.3    Wang, Y.4    Mizuki, M.5    Kanakura, Y.6    Besmer, P.7    Neel, B.G.8    Gu, H.9
  • 19
    • 0036530214 scopus 로고    scopus 로고
    • 1-integrin signaling pathway-mediated hematopoietic cell adhesion and migration
    • DOI 10.1182/blood.V99.7.2351
    • Yu WM, Hawley TS, Hawley RG & Qu CK (2002) Role of the docking protein Gab2 in beta(1)-integrin signaling pathway-mediated hematopoietic cell adhesion and migration. Blood 99, 2351-2359. (Pubitemid 34525420)
    • (2002) Blood , vol.99 , Issue.7 , pp. 2351-2359
    • Yu, W.-M.1    Hawley, T.S.2    Hawley, R.G.3    Qu, C.-K.4
  • 20
    • 2342418250 scopus 로고    scopus 로고
    • Gab1 Contributes to Cytoskeletal Reorganization and Chemotaxis in Response to Platelet-derived Growth Factor
    • DOI 10.1074/jbc.M312996200
    • Kallin A, Demoulin JB, Nishida K, Hirano T, Ronnstrand L & Heldin CH (2004) Gab1 contributes to cytoskeletal reorganization and chemotaxis in response to platelet-derived growth factor. J Biol Chem 279, 17897-17904. (Pubitemid 38560558)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17897-17904
    • Kallin, A.1    Demoulin, J.-B.2    Nishida, K.3    Hirano, T.4    Ronnstrand, L.5    Heldin, C.-H.6
  • 23
    • 0033576621 scopus 로고    scopus 로고
    • Met-induced JNK activation is mediated by the adapter protein Crk and correlates with the Gab1-Crk signaling complex formation
    • Garcia-Guzman M, Dolfi F, Zeh K & Vuori K (1999) Met-induced JNK activation is mediated by the adapter protein Crk and correlates with the Gab1-Crk signaling complex formation. Oncogene 18, 7775-7786. (Pubitemid 30052762)
    • (1999) Oncogene , vol.18 , Issue.54 , pp. 7775-7786
    • Garcia-Guzman, M.1    Dolfi, F.2    Zeh, K.3    Vuori, K.4
  • 24
    • 0034646610 scopus 로고    scopus 로고
    • Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rap1 via the large docking protein Gab1 and the adapter protein CRKL
    • DOI 10.1074/jbc.275.15.10772
    • Sakkab D, Lewitzky M, Posern G, Schaeper U, Sachs M, Birchmeier W & Feller SM (2000) Signaling of hepatocyte growth factor/scatter factor (HGF) to the small GTPase Rap1 via the large docking protein Gab1 and the adapter protein CRKL. J Biol Chem 275, 10772-10778. (Pubitemid 30212706)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 10772-10778
    • Sakkab, D.1    Lewitzky, M.2    Posern, G.3    Schaeper, U.4    Sachs, M.5    Birchmeier, W.6    Feller, S.M.7
  • 25
    • 33746888255 scopus 로고    scopus 로고
    • Adaptor molecule Crk is required for sustained phosphorylation of Grb2-associated binder 1 and hepatocyte growth factor-induced cell motility of human synovial sarcoma cell lines
    • DOI 10.1158/1541-7786.MCR-05-0141
    • Watanabe T, Tsuda M, Makino Y, Ichihara S, Sawa H, Minami A, Mochizuki N, Nagashima K & Tanaka S (2006) Adaptor molecule Crk is required for sustained phosphorylation of Grb2-associated binder 1 and hepatocyte growth factor-induced cell motility of human synovial sarcoma cell lines. Mol Cancer Res 4, 499-510. (Pubitemid 44197045)
    • (2006) Molecular Cancer Research , vol.4 , Issue.7 , pp. 499-510
    • Watanabe, T.1    Tsuda, M.2    Makino, Y.3    Ichihara, S.4    Sawa, H.5    Minami, A.6    Mochizuki, N.7    Nagashima, K.8    Tanaka, S.9
  • 26
    • 0037020180 scopus 로고    scopus 로고
    • Crk synergizes with epidermal growth factor for epithelial invasion and morphogenesis and is required for the met morphogenic program
    • Lamorte L, Rodrigues S, Naujokas M & Park M (2002) Crk synergizes with epidermal growth factor for epithelial invasion and morphogenesis and is required for the met morphogenic program. J Biol Chem 277, 37904-37911.
    • (2002) J Biol Chem , vol.277 , pp. 37904-37911
    • Lamorte, L.1    Rodrigues, S.2    Naujokas, M.3    Park, M.4
  • 27
    • 0036258332 scopus 로고    scopus 로고
    • Receptor-specific regulation of phosphatidylinositol 3′-kinase activation by the protein tyrosine phosphatase Shp2
    • DOI 10.1128/MCB.22.12.4062-4072.2002
    • Zhang SQ, Tsiaras WG, Araki T, Wen G, Minichiello L, Klein R & Neel BG (2002) Receptor-specific regulation of phosphatidylinositol 3¢-kinase activation by the protein tyrosine phosphatase Shp2. Mol Cell Biol 22, 4062-4072. (Pubitemid 34556577)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.12 , pp. 4062-4072
    • Zhang, S.Q.1    Tsiaras, W.G.2    Araki, T.3    Wen, G.4    Minichiello, L.5    Klein, R.6    Neel, B.G.7
  • 28
    • 4644275694 scopus 로고    scopus 로고
    • Phosphorylation of Grb2-associated binder 2 on serine 623 by ERK MAPK regulates its association with the phosphatase SHP-2 and decreases STAT5 activation
    • Arnaud M, Crouin C, Deon C, Loyaux D & Bertoglio J (2004) Phosphorylation of Grb2-associated binder 2 on serine 623 by ERK MAPK regulates its association with the phosphatase SHP-2 and decreases STAT5 activation. J Immunol 173, 3962-3971. (Pubitemid 39280760)
    • (2004) Journal of Immunology , vol.173 , Issue.6 , pp. 3962-3971
    • Arnaud, M.1    Crouin, C.2    Deon, C.3    Loyaux, D.4    Bertoglio, J.5
  • 29
    • 0037080536 scopus 로고    scopus 로고
    • PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2
    • DOI 10.1093/emboj/21.1.72
    • Lynch DK & Daly RJ (2002) PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2. EMBO J 21, 72-82. (Pubitemid 34087076)
    • (2002) EMBO Journal , vol.21 , Issue.1-2 , pp. 72-82
    • Lynch, D.K.1    Daly, R.J.2
  • 32
    • 0033624921 scopus 로고    scopus 로고
    • Role of Gab l in heart, placenta, and skin development and growth factor- And cytokine-induced extracellular signal-regulated kinase mitogen- activated protein kinase activation
    • DOI 10.1128/MCB.20.10.3695-3704.2000
    • Itoh M, Yoshida Y, Nishida K, Narimatsu M, Hibi M & Hirano T (2000) Role of Gab1 in heart, placenta, and skin development and growth factor- and cytokine- induced extracellular signal-regulated kinase mitogen- activated protein kinase activation. Mol Cell Biol 20, 3695-3704. (Pubitemid 30243915)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.10 , pp. 3695-3704
    • Itoh, M.1    Yoshida, Y.2    Nishida, K.3    Narimatsu, M.4    Hibi, M.5    Hirano, T.6
  • 43
    • 34250180190 scopus 로고    scopus 로고
    • Increased expression of Gab2, a scaffolding adaptor of the tyrosine kinase signalling, in gastric carcinomas
    • DOI 10.1080/00313020701329773, PII 779274065
    • Lee SH, Jeong EG, Nam SW, Lee JY, Yoo NJ & Lee SH (2007) Increased expression of Gab2, a scaffolding adaptor of the tyrosine kinase signalling, in gastric carcinomas. Pathology 39, 326-329. (Pubitemid 46897604)
    • (2007) Pathology , vol.39 , Issue.3 , pp. 326-329
    • Lee, S.H.1    Jeong, E.G.2    Nam, S.W.3    Lee, J.Y.4    Yoo, N.J.5    Lee, S.H.6
  • 49
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara H, Hadari YR, Spivak-Kroizman T, Schilling J, Bar-Sagi D, Lax I & Schlessinger J (1997) A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell 89, 693-702. (Pubitemid 27516172)
    • (1997) Cell , vol.89 , Issue.5 , pp. 693-702
    • Kouhara, H.1    Hadari, Y.R.2    Spivak-Kroizman, T.3    Schilling, J.4    Bar-Sagi, D.5    Lax, I.6    Schlessinger, J.7
  • 50
    • 0037853219 scopus 로고    scopus 로고
    • Fibroblast growth factor-2-induced signaling through lipid raft-associated fibroblast growth factor receptor substrate 2 (FRS2)
    • DOI 10.1074/jbc.M210245200
    • Ridyard MS & Robbins SM (2003) Fibroblast growth factor-2-induced signaling through lipid raft-associated fibroblast growth factor receptor substrate 2 (FRS2). J Biol Chem 278, 13803-13809. (Pubitemid 36799918)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 13803-13809
    • Ridyard, M.S.1    Robbins, S.M.2
  • 51
    • 42449122262 scopus 로고    scopus 로고
    • Differential membrane compartmentalization of Ret by PTB-adaptor engagement
    • DOI 10.1111/j.1742-4658.2008.06360.x
    • Lundgren TK, Luebke M, Stenqvist A & Ernfors P (2008) Differential membrane compartmentalization of Ret by PTB-adaptor engagement. FEBS J 275, 2055-2066. (Pubitemid 351569547)
    • (2008) FEBS Journal , vol.275 , Issue.9 , pp. 2055-2066
    • Lundgren, T.K.1    Luebke, M.2    Stenqvist, A.3    Ernfors, P.4
  • 52
    • 0034865053 scopus 로고    scopus 로고
    • Xenopus FRS2 is involved in early embryogenesis in cooperation with the Src family kinase Laloo
    • DOI 10.1093/embo-reports/kve152
    • Kusakabe M, Masuyama N, Hanafusa H & Nishida E (2001) Xenopus FRS2 is involved in early embryogene- sis in cooperation with the Src family kinase Laloo. EMBO Report 2, 727-735. (Pubitemid 32798717)
    • (2001) EMBO Reports , vol.2 , Issue.8 , pp. 727-735
    • Kusakabe, M.1    Masuyama, N.2    Hanafusa, H.3    Nishida, E.4
  • 53
    • 0034747206 scopus 로고    scopus 로고
    • SNT-1/FRS2alpha physically interacts with Laloo and mediates mesoderm induction by fibroblast growth factor
    • DOI 10.1016/S0925-4773(01)00524-X, PII S092547730100524X
    • Hama J, Xu H, Goldfarb M & Weinstein DC (2001) SNT-1/FRS2alpha physically interacts with Laloo and mediates mesoderm induction by fibroblast growth factor. Mech Dev 109, 195-204. (Pubitemid 33112032)
    • (2001) Mechanisms of Development , vol.109 , Issue.2 , pp. 195-204
    • Hama, J.1    Xu, H.2    Goldfarb, M.3    Weinstein, D.C.4
  • 54
    • 0033974109 scopus 로고    scopus 로고
    • FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors
    • DOI 10.1128/MCB.20.3.979-989.2000
    • Ong SH, Guy GR, Hadari YR, Laks S, Gotoh N, Schlessinger J & Lax I (2000) FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. Mol Cell Biol 20, 979-989. (Pubitemid 30044235)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.3 , pp. 979-989
    • Ong, S.H.1    Guy, G.R.2    Hadari, Y.R.3    Laks, S.4    Gotoh, N.5    Schlessinger, J.6    Lax, I.7
  • 55
    • 0035848684 scopus 로고    scopus 로고
    • Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction
    • DOI 10.1038/sj.onc.1204290
    • Kurokawa K, Iwashita T, Murakami H, Hayashi H, Kawai K & Takahashi M (2001) Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction. Oncogene 20, 1929-1938. (Pubitemid 32458025)
    • (2001) Oncogene , vol.20 , Issue.16 , pp. 1929-1938
    • Kurokawa, K.1    Iwashita, T.2    Murakami, H.3    Hayashi, H.4    Kawai, K.5    Takahashi, M.6
  • 57
    • 33750214274 scopus 로고    scopus 로고
    • Unique role of SNT-2/FRS2beta/FRS3 docking/adaptor protein for negative regulation in EGF receptor tyrosine kinase signaling pathways
    • DOI 10.1038/sj.onc.1209656, PII 1209656
    • Huang L, Watanabe M, Chikamori M, Kido Y, Yamamoto T, Shibuya M, Gotoh N & Tsuchida N (2006) Unique role of SNT-2/FRS2beta/FRS3 docking /adaptor protein for negative regulation in EGF receptor tyrosine kinase signaling pathways. Oncogene 25, 6457-6466. (Pubitemid 44607078)
    • (2006) Oncogene , vol.25 , Issue.49 , pp. 6457-6466
    • Huang, L.1    Watanabe, M.2    Chikamori, M.3    Kido, Y.4    Yamamoto, T.5    Shibuya, M.6    Gotoh, N.7    Tsuchida, N.8
  • 61
    • 11244251791 scopus 로고    scopus 로고
    • Direct cell cycle regulation by the fibroblast growth factor receptor (FGFR) kinase through phosphorylation-dependent release of Cks1 from FGFR substrate 2
    • DOI 10.1074/jbc.M409230200
    • Zhang Y, Lin Y, Bowles C & Wang F (2004) Direct cell cycle regulation by the fibroblast growth factor receptor (FGFR) kinase through phosphorylationdependent release of Cks1 from FGFR substrate 2. J Biol Chem 279, 55348-55354. (Pubitemid 40066533)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55348-55354
    • Zhang, Y.1    Lin, Y.2    Bowles, C.3    Wang, F.4
  • 62
    • 24044544231 scopus 로고    scopus 로고
    • Direct interaction of Rnd1 with FRS2beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells
    • DOI 10.1074/jbc.M411356200
    • Harada A, Katoh H & Negishi M (2005) Direct interaction of Rnd1 with FRS2 beta regulates Rnd1- induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells. J Biol Chem 280, 18418-18424. (Pubitemid 41389091)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 18418-18424
    • Harada, A.1    Katoh, H.2    Negishi, M.3
  • 63
    • 12344278405 scopus 로고    scopus 로고
    • FRS2-dependent SRC activation is required for fibroblast growth factor receptor-induced phosphorylation of Sprouty and suppression of ERK activity
    • DOI 10.1242/jcs.01519
    • Li X, Brunton VG, Burgar HR, Wheldon LM & Heath JK (2004) FRS2-dependent SRC activation is required for fibroblast growth factor receptor-induced phosphorylation of Sprouty and suppression of ERK activity. J Cell Sci 117, 6007-6017. (Pubitemid 40123967)
    • (2004) Journal of Cell Science , vol.117 , Issue.25 , pp. 6007-6017
    • Li, X.1    Brunton, V.G.2    Burgar, H.R.3    Wheldon, L.M.4    Heath, J.K.5
  • 64
    • 0036771763 scopus 로고    scopus 로고
    • The docking protein FRS2alpha controls a MAP kinase-mediated negative feedback mechanism for signaling by FGF receptors
    • DOI 10.1016/S1097-2765(02)00689-5
    • Lax I, Wong A, Lamothe B, Lee A, Frost A, Hawes J & Schlessinger J (2002) The docking protein FRS2alpha controls a MAP kinase-mediated negative feedback mechanism for signaling by FGF receptors. Mol Cell 10, 709-719. (Pubitemid 35335628)
    • (2002) Molecular Cell , vol.10 , Issue.4 , pp. 709-719
    • Lax, I.1    Wong, A.2    Lamothe, B.3    Lee, A.4    Frost, A.5    Hawes, J.6    Schlessinger, J.7
  • 68
    • 38349026317 scopus 로고    scopus 로고
    • Characterization of the 12q amplicons by high-resolution, oligonucleotide array CGH and expression analyses of a novel liposarcoma cell line
    • Persson F, Olofsson A, Sjogren H, Chebbo N, Nilsson B, Stenman G & Aman P (2008) Characterization of the 12q amplicons by high-resolution, oligonucleotide array CGH and expression analyses of a novel liposarcoma cell line. Cancer Lett 260, 37-47.
    • (2008) Cancer Lett , vol.260 , pp. 37-47
    • Persson, F.1    Olofsson, A.2    Sjogren, H.3    Chebbo, N.4    Nilsson, B.5    Stenman, G.6    Aman, P.7
  • 71
    • 0022347547 scopus 로고
    • Insulin rapidly stimulates tyrosine phosphorylation of a M(r)-185,000 protein in intact cells
    • DOI 10.1038/318183a0
    • White MF, Maron R & Kahn CR (1985) Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells. Nature 318, 183-186. (Pubitemid 16192587)
    • (1985) Nature , vol.318 , Issue.6042 , pp. 183-186
    • White, M.F.1    Maron, R.2    Kahn, C.R.3
  • 73
    • 0034463086 scopus 로고    scopus 로고
    • Different subcellular localization and phosphoinositides binding of insulin receptor substrate protein pleckstrin homology domains
    • DOI 10.1210/me.14.6.823
    • Razzini G, Ingrosso A, Brancaccio A, Sciacchitano S, Esposito DL & Falasca M (2000) Different subcellular localization and phosphoinositides binding of insulin receptor substrate protein pleckstrin homology domains. Mol Endocrinol 14, 823-836. (Pubitemid 32260496)
    • (2000) Molecular Endocrinology , vol.14 , Issue.6 , pp. 823-836
    • Razzini, G.1    Ingrosso, A.2    Brancaccio, A.3    Sciacchitano, S.4    Esposito, D.L.5    Falasca, M.6
  • 74
    • 0030611578 scopus 로고    scopus 로고
    • In vitro binding and phosphorylation of insulin receptor substrate 1 by the insulin receptor. Role of interactions mediated by the phosphotyrosine- binding domain and the pleckstrin-homology domain
    • Backer JM, Wjasow C & Zhang Y (1997) In vitro binding and phosphorylation of insulin receptor substrate 1 by the insulin receptor. Role of interactions mediated by the phosphotyrosine-binding domain and the pleckstrin-homology domain. Eur J Biochem 245, 91-96.
    • (1997) Eur J Biochem , vol.245 , pp. 91-96
    • Backer, J.M.1    Wjasow, C.2    Zhang, Y.3
  • 75
    • 0030010590 scopus 로고    scopus 로고
    • Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor
    • DOI 10.1016/S0092-8674(00)81236-2
    • Eck MJ, Dhe-Paganon S, Trub T, Nolte RT & Shoelson SE (1996) Structure of the IRS-1 PTB domain bound to the juxtamembrane region of the insulin receptor. Cell 85, 695-705. (Pubitemid 26181049)
    • (1996) Cell , vol.85 , Issue.5 , pp. 695-705
    • Eck, M.J.1    Dhe-Paganon, S.2    Trub, T.3    Nolle, R.T.4    Shoelson, S.E.5
  • 76
    • 0030611168 scopus 로고    scopus 로고
    • 628in insulin receptor substrate-2 mediate its association with the insulin receptor
    • DOI 10.1074/jbc.272.26.16414
    • Sawka-Verhelle D, Baron V, Mothe I, Filloux C, White MF & Van Obberghen E (1997) Tyr624 and Tyr628 in insulin receptor substrate-2 mediate its association with the insulin receptor. J Biol Chem 272, 16414-16420. (Pubitemid 27276467)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16414-16420
    • Sawka-Verhelle, D.1    Baron, V.2    Mothe, I.3    Filloux, C.4    White, M.F.5    Van, O.E.6
  • 80
    • 0028909206 scopus 로고
    • Regulation of phosphatidylinositol 3¢-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit
    • Rordorf-Nikolic T, Van Horn DJ, Chen D, White MF & Backer JM (1995) Regulation of phosphatidylinositol 3¢-kinase by tyrosyl phosphoproteins. Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit. J Biol Chem 270, 3662-3666.
    • (1995) J Biol Chem , vol.270 , pp. 3662-3666
    • Rordorf-Nikolic, T.1    Van Horn, D.J.2    Chen, D.3    White, M.F.4    Backer, J.M.5
  • 81
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: Insights into insulin action
    • DOI 10.1038/nrm1837, PII NRM1837
    • Taniguchi CM, Emanuelli B & Kahn CR (2006) Critical nodes in signalling pathways: insights into insulin action. Nat Rev Mol Cell Biol 7, 85-96. (Pubitemid 43278292)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.2 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 82
    • 0035856949 scopus 로고    scopus 로고
    • Insulin signalling and the regulation of glucose and lipid metabolism
    • DOI 10.1038/414799a
    • Saltiel AR & Kahn CR (2001) Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414, 799-806. (Pubitemid 34000783)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 799-806
    • Saltiel, A.R.1    Kahn, C.R.2
  • 85
    • 15644368839 scopus 로고    scopus 로고
    • The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling
    • DOI 10.1074/jbc.273.41.26908
    • Myers MG Jr, Mendez R, Shi P, Pierce JH, Rhoads R & White MF (1998) The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling. J Biol Chem 273, 26908-26914. (Pubitemid 28471711)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26908-26914
    • Myers Jr., M.G.1    Mendez, R.2    Shi, P.3    Pierce, J.H.4    Rhoads, R.5    White, M.F.6
  • 88
    • 0033988375 scopus 로고    scopus 로고
    • IRS-4 mediates protein kinase B signaling during insulin stimulation without promoting antiapoptosis
    • Uchida T, Myers MG Jr & White MF (2000) IRS-4 mediates protein kinase B signaling during insulin stimulation without promoting antiapoptosis. Mol Cell Biol 20, 126-138. (Pubitemid 30002554)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.1 , pp. 126-138
    • Uchida, T.1    Myers Jr., M.G.2    White, M.F.3
  • 89
    • 0030730246 scopus 로고    scopus 로고
    • Cloning, tissue expression, and chromosomal localization of the mouse IRS-3 gene
    • DOI 10.1210/en.138.11.4931
    • Sciacchitano S & Taylor SI (1997) Cloning, tissue expression, and chromosomal localization of the mouse IRS-3 gene. Endocrinology 138, 4931-4940. (Pubitemid 27460933)
    • (1997) Endocrinology , vol.138 , Issue.11 , pp. 4931-4940
    • Sciacchitano, S.1    Taylor, S.I.2
  • 93
    • 0032841435 scopus 로고    scopus 로고
    • Irs-2 coordinates Igf-1 receptor-mediated beta-cell development and peripheral insulin signalling
    • DOI 10.1038/12631
    • Withers DJ, Burks DJ, Towery HH, Altamuro SL, Flint CL & White MF (1999) Irs-2 coordinates Igf-1 receptor-mediated beta-cell development and peripheral insulin signalling. Nat Genet 23, 32-40. (Pubitemid 29418784)
    • (1999) Nature Genetics , vol.23 , Issue.1 , pp. 32-40
    • Withers, D.J.1    Burks, D.J.2    Towery, H.H.3    Altamuro, S.L.4    Flint, C.L.5    White, M.F.6
  • 94
    • 0033581023 scopus 로고    scopus 로고
    • Insulin receptor substrate 3 is not essential for growth or glucose homeostasis
    • Liu SC, Wang Q, Lienhard GE & Keller SR (1999) Insulin receptor substrate 3 is not essential for growth or glucose homeostasis. J Biol Chem 274, 18093-18099.
    • (1999) J Biol Chem , vol.274 , pp. 18093-18099
    • Liu, S.C.1    Wang, Q.2    Lienhard, G.E.3    Keller, S.R.4
  • 95
    • 33745668478 scopus 로고    scopus 로고
    • SiRNA-based gene silencing reveals specialized roles of IRS-1/Akt2 and IRS-2/Akt1 in glucose and lipid metabolism in human skeletal muscle
    • DOI 10.1016/j.cmet.2006.04.008, PII S1550413106001276
    • Bouzakri K, Zachrisson A, Al-Khalili L, Zhang BB, Koistinen HA, Krook A & Zierath JR (2006) siRNA-based gene silencing reveals specialized roles of IRS-1/Akt2 and IRS-2/Akt1 in glucose and lipid metabolism in human skeletal muscle. Cell Metab 4, 89-96. (Pubitemid 43964475)
    • (2006) Cell Metabolism , vol.4 , Issue.1 , pp. 89-96
    • Bouzakri, K.1    Zachrisson, A.2    Al-Khalili, L.3    Zhang, B.B.4    Koistinen, H.A.5    Krook, A.6    Zierath, J.R.7
  • 96
    • 18044382930 scopus 로고    scopus 로고
    • Atypical protein kinase C in insulin action and insulin resistance
    • DOI 10.1042/BST0330350
    • Farese RV, Sajan MP & Standaert ML (2005) Atypical protein kinase C in insulin action and insulin resistance. Biochem Soc Trans 33, 350-353. (Pubitemid 40604370)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.2 , pp. 350-353
    • Farese, R.V.1    Sajan, M.P.2    Standaert, M.L.3
  • 97
    • 65649098029 scopus 로고    scopus 로고
    • Phosphorylation of IRS proteins, insulin action, and insulin resistance
    • Boura-Halfon S & Zick Y (2009) Phosphorylation of IRS proteins, insulin action, and insulin resistance. Am J Physiol 296, E581-591.
    • (2009) Am J Physiol , vol.296
    • Boura-Halfon, S.1    Zick, Y.2
  • 99
    • 0034708832 scopus 로고    scopus 로고
    • The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307)
    • Aguirre V, Uchida T, Yenush L, Davis R & White MF (2000) The c-Jun NH(2)-terminal kinase promotes insulin resistance during association with insulin receptor substrate-1 and phosphorylation of Ser(307). J Biol Chem 275, 9047-9054.
    • (2000) J Biol Chem , vol.275 , pp. 9047-9054
    • Aguirre, V.1    Uchida, T.2    Yenush, L.3    Davis, R.4    White, M.F.5
  • 100
    • 0037073679 scopus 로고    scopus 로고
    • Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappaB kinase complex
    • DOI 10.1074/jbc.M209459200
    • Gao Z, Hwang D, Bataille F, Lefevre M, York D, Quon MJ & Ye J (2002) Serine phosphorylation of insulin receptor substrate 1 by inhibitor kappa B kinase complex. J Biol Chem 277, 48115-48121. (Pubitemid 35470759)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48115-48121
    • Gao, Z.1    Hwang, D.2    Bataille, F.3    Lefevre, M.4    York, D.5    Quon, M.J.6    Ye, J.7
  • 101
    • 0030931560 scopus 로고    scopus 로고
    • Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action
    • Eldar-Finkelman H & Krebs EG (1997) Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action. Proc Natl Acad Sci USA 94, 9660-9664.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9660-9664
    • Eldar-Finkelman, H.1    Krebs, E.G.2
  • 102
    • 48249089367 scopus 로고    scopus 로고
    • Protein kinase C function in muscle, liver, and beta-cells and its therapeutic implications for type 2 diabetes
    • Schmitz-Peiffer C & Biden TJ (2008) Protein kinase C function in muscle, liver, and beta-cells and its therapeutic implications for type 2 diabetes. Diabetes 57, 1774-1783.
    • (2008) Diabetes , vol.57 , pp. 1774-1783
    • Schmitz-Peiffer, C.1    Biden, T.J.2
  • 103
    • 0037059330 scopus 로고    scopus 로고
    • 307in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action
    • DOI 10.1074/jbc.M101521200
    • Aguirre V, Werner ED, Giraud J, Lee YH, Shoelson SE & White MF (2002) Phosphorylation of Ser307 in insulin receptor substrate-1 blocks interactions with the insulin receptor and inhibits insulin action. J Biol Chem 277, 1531-1537. (Pubitemid 34968910)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 1531-1537
    • Aguirre, V.1    Werner, E.D.2    Giraud, J.3    Lee, Y.H.4    Shoelson, S.E.5    White, M.F.6
  • 105
    • 0038321436 scopus 로고    scopus 로고
    • Reduced activation of phosphatidylinositol-3 kinase and increased serine 636 phosphorylation of insulin receptor substrate-1 in primary culture of skeletal muscle cells from patients with type 2 diabetes
    • DOI 10.2337/diabetes.52.6.1319
    • Bouzakri K, Roques M, Gual P, Espinosa S, Guebre- Egziabher F, Riou JP, Laville M, Le Marchand-Brustel Y, Tanti JF & Vidal H (2003) Reduced activation of phosphatidylinositol-3 kinase and increased serine 636 phosphorylation of insulin receptor substrate-1 in primary culture of skeletal muscle cells from patients with type 2 diabetes. Diabetes 52, 1319-1325. (Pubitemid 36666183)
    • (2003) Diabetes , vol.52 , Issue.6 , pp. 1319-1325
    • Bouzakri, K.1    Roques, M.2    Gual, P.3    Espinosa, S.4    Guebre-Egziabher, F.5    Riou, J.-P.6    Laville, M.7    Le, M.-B.Y.8    Tanti, J.-F.9    Vidal, H.10
  • 107
    • 42449104397 scopus 로고    scopus 로고
    • Protein kinase C-zeta phosphorylates insulin receptor substrate- 1, -3, and -4 but not -2: Isoform specific determinants of specificity in insulin signaling
    • Lee S, Lynn EG, Kim JA & Quon MJ (2008) Protein kinase C-zeta phosphorylates insulin receptor substrate- 1, -3, and -4 but not -2: isoform specific determinants of specificity in insulin signaling. Endocrinology 149, 2451-2458.
    • (2008) Endocrinology , vol.149 , pp. 2451-2458
    • Lee, S.1    Lynn, E.G.2    Kim, J.A.3    Quon, M.J.4
  • 108
    • 0344298921 scopus 로고    scopus 로고
    • Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle
    • DOI 10.2337/diabetes.48.8.1562
    • Patti ME, Virkamaki A, Landaker EJ, Kahn CR & Yki-Jarvinen H (1999) Activation of the hexosamine pathway by glucosamine in vivo induces insulin resistance of early postreceptor insulin signaling events in skeletal muscle. Diabetes 48, 1562-1571. (Pubitemid 29356864)
    • (1999) Diabetes , vol.48 , Issue.8 , pp. 1562-1571
    • Patti, M.-E.1    Virkamaki, A.2    Landaker, E.J.3    Kahn, C.R.4    Yki-Jarvinen, H.5
  • 110
    • 13844272212 scopus 로고    scopus 로고
    • Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation
    • Kaiser C & James SR (2004) Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation. BMC Biol 2, 23.
    • (2004) BMC Biol , vol.2 , pp. 23
    • Kaiser, C.1    James, S.R.2
  • 111
    • 36348974168 scopus 로고    scopus 로고
    • The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation
    • Zhang J (2007) The direct involvement of SirT1 in insulin-induced insulin receptor substrate-2 tyrosine phosphorylation. J Biol Chem 282, 34356-34364.
    • (2007) J Biol Chem , vol.282 , pp. 34356-34364
    • Zhang, J.1
  • 112
    • 69249217275 scopus 로고    scopus 로고
    • Expression and function of the insulin receptor substrate proteins in cancer
    • Mardilovich K, Pankratz SL & Shaw LM (2009) Expression and function of the insulin receptor substrate proteins in cancer. Cell Commun Signal 7, 14.
    • (2009) Cell Commun Signal , vol.7 , pp. 14
    • Mardilovich, K.1    Pankratz, S.L.2    Shaw, L.M.3
  • 113
    • 7644237126 scopus 로고    scopus 로고
    • Involvement of insulin receptor substrate 2 in mammary tumor metastasis
    • DOI 10.1128/MCB.24.22.9726-9735.2004
    • Nagle JA, Ma Z, Byrne MA, White MF & Shaw LM (2004) Involvement of insulin receptor substrate 2 in mammary tumor metastasis. Mol Cell Biol 24, 9726-9735. (Pubitemid 39458801)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.22 , pp. 9726-9735
    • Nagle, J.A.1    Ma, Z.2    Byrne, M.A.3    White, M.F.4    Shaw, L.M.5
  • 114
    • 70350406465 scopus 로고    scopus 로고
    • The roles of Dok family adapters in immunoreceptor signaling
    • Mashima R, Hishida Y, Tezuka T & Yamanashi Y (2009) The roles of Dok family adapters in immunoreceptor signaling. Immunol Rev 232, 273-285.
    • (2009) Immunol Rev , vol.232 , pp. 273-285
    • Mashima, R.1    Hishida, Y.2    Tezuka, T.3    Yamanashi, Y.4
  • 115
    • 32244441418 scopus 로고    scopus 로고
    • Drosophila Dok is required for embryonic dorsal closure
    • DOI 10.1242/dev.02198
    • Biswas R, Stein D & Stanley ER (2006) Drosophila Dok is required for embryonic dorsal closure. Development 133, 217-227. (Pubitemid 43210711)
    • (2006) Development , vol.133 , Issue.2 , pp. 217-227
    • Biswas, R.1    Stein, D.2    Stanley, E.R.3
  • 116
    • 0031444245 scopus 로고    scopus 로고
    • Identification of the Abl- And rasGAP-associated 62 kDa protein as a docking protein, dok
    • DOI 10.1016/S0092-8674(00)81841-3
    • Yamanashi Y & Baltimore D (1997) Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok. Cell 88, 205-211. (Pubitemid 28015869)
    • (1997) Cell , vol.88 , Issue.2 , pp. 205-211
    • Yamanashi, Y.1    Baltimore, D.2
  • 117
    • 0031459864 scopus 로고    scopus 로고
    • P62(dok): A constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells
    • Carpino N, Wisniewski D, Strife A, Marshak D, Kobayashi R, Stillman B & Clarkson B (1997) p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 88, 197-204.
    • (1997) Cell , vol.88 , pp. 197-204
    • Carpino, N.1    Wisniewski, D.2    Strife, A.3    Marshak, D.4    Kobayashi, R.5    Stillman, B.6    Clarkson, B.7
  • 120
    • 33847240085 scopus 로고    scopus 로고
    • Subcellular localization of Grb2 by the adaptor protein Dok- 3 restricts the intensity of Ca2+ signaling in B cells
    • Stork B, Neumann K, Goldbeck I, Alers S, Kahne T, Naumann M, Engelke M & Wienands J (2007) Subcellular localization of Grb2 by the adaptor protein Dok- 3 restricts the intensity of Ca2+ signaling in B cells. EMBO J 26, 1140-1149.
    • (2007) EMBO J , vol.26 , pp. 1140-1149
    • Stork, B.1    Neumann, K.2    Goldbeck, I.3    Alers, S.4    Kahne, T.5    Naumann, M.6    Engelke, M.7    Wienands, J.8
  • 121
    • 2442458850 scopus 로고    scopus 로고
    • Pleckstrin Homology and Phosphotyrosine-binding Domain-dependent Membrane Association and Tyrosine Phosphorylation of Dok-4, an Inhibitory Adapter Molecule Expressed in Epithelial Cells
    • DOI 10.1074/jbc.M310689200
    • Bedirian A, Baldwin C, Abe J, Takano T & Lemay S (2004) Pleckstrin homology and phosphotyrosine-binding domain-dependent membrane association and tyrosine phosphorylation of Dok-4, an inhibitory adapter molecule expressed in epithelial cells. J Biol Chem 279, 19335-19349. (Pubitemid 38623365)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 19335-19349
    • Bedirian, A.1    Baldwin, C.2    Abe, J.-I.3    Takano, T.4    Lemay, S.5
  • 123
    • 44349112262 scopus 로고    scopus 로고
    • Constitutive plasma membrane targeting and microdomain localization of Dok5 studied by single-molecule microscopy
    • Fu G, Zhang F, Cao L, Xu ZZ, Chen YZ, Wang GY & He C (2008) Constitutive plasma membrane targeting and microdomain localization of Dok5 studied by single-molecule microscopy. Biophys Chem 136, 13-18.
    • (2008) Biophys Chem , vol.136 , pp. 13-18
    • Fu, G.1    Zhang, F.2    Cao, L.3    Xu, Z.Z.4    Chen, Y.Z.5    Wang, G.Y.6    He, C.7
  • 126
    • 0033598172 scopus 로고    scopus 로고
    • Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation
    • DOI 10.1016/S0960-9822(99)80458-8
    • Jones N & Dumont DJ (1999) Recruitment of Dok-R to the EGF receptor through its PTB domain is required for attenuation of Erk MAP kinase activation. Curr Biol 9, 1057-1060. (Pubitemid 29456178)
    • (1999) Current Biology , vol.9 , Issue.18 , pp. 1057-1060
    • Jones, N.1    Dumont, D.J.2
  • 127
    • 25444456370 scopus 로고    scopus 로고
    • Phosphotyrosine binding-mediated oligomerization of downstream of tyrosine kinase (Dok)-1 and Dok-2 is involved in CD2-induced Dok phosphorylation
    • Boulay I, Nemorin JG & Duplay P (2005) Phosphotyrosine binding-mediated oligomerization of downstream of tyrosine kinase (Dok)-1 and Dok-2 is involved in CD2-induced Dok phosphorylation. J Immunol 175, 4483-4489. (Pubitemid 41361985)
    • (2005) Journal of Immunology , vol.175 , Issue.7 , pp. 4483-4489
    • Boulay, I.1    Nemorin, J.-G.2    Duplay, P.3
  • 128
    • 0035951773 scopus 로고    scopus 로고
    • Domain-dependent function of the rasGAPbinding protein p62Dok in cell signaling
    • Songyang Z, Yamanashi Y, Liu D & Baltimore D (2001) Domain-dependent function of the rasGAPbinding protein p62Dok in cell signaling. J Biol Chem 276, 2459-2465.
    • (2001) J Biol Chem , vol.276 , pp. 2459-2465
    • Songyang, Z.1    Yamanashi, Y.2    Liu, D.3    Baltimore, D.4
  • 130
    • 0035939661 scopus 로고    scopus 로고
    • Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation
    • DOI 10.1083/jcb.200102032
    • Grimm J, Sachs M, Britsch S, Di Cesare S, Schwarz- Romond T, Alitalo K & Birchmeier W (2001) Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation. J Cell Biol 154, 345-354. (Pubitemid 34286145)
    • (2001) Journal of Cell Biology , vol.154 , Issue.2 , pp. 345-354
    • Grimm, J.1    Sachs, M.2    Britsch, S.3    Di, C.S.4    Schwarz-Romond, T.5    Alitalo, K.6    Birchmeier, W.7
  • 131
    • 34347407347 scopus 로고    scopus 로고
    • Dok-3 plays a nonredundant role in negative regulation of B-cell activation
    • DOI 10.1182/blood-2006-10-055194
    • Ng CH, Xu S & Lam KP (2007) Dok-3 plays a nonredundant role in negative regulation of B-cell activation. Blood 110, 259-266. (Pubitemid 47026843)
    • (2007) Blood , vol.110 , Issue.1 , pp. 259-266
    • Ng, C.-H.1    Xu, S.2    Lam, K.-P.3
  • 136
    • 77952538099 scopus 로고    scopus 로고
    • Dok-7 promotes slow muscle integrity as well as neuromuscular junction formation in a zebrafish model of congenital myasthenic syndromes
    • Muller JS, Jepson CD, Laval SH, Bushby K, Straub V & Lochmuller H (2010) Dok-7 promotes slow muscle integrity as well as neuromuscular junction formation in a zebrafish model of congenital myasthenic syndromes. Human Mol Genet 19, 1726-1740.
    • (2010) Human Mol Genet , vol.19 , pp. 1726-1740
    • Muller, J.S.1    Jepson, C.D.2    Laval, S.H.3    Bushby, K.4    Straub, V.5    Lochmuller, H.6


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