메뉴 건너뛰기




Volumn 28, Issue 2, 2003, Pages 79-91

Involvement of Crk Adapter Proteins in Regulation of Lymphoid Cell Functions

Author keywords

Adapter protein; Cbl; Crk; Lymphocyte activation; Signal transduction; Src homology 2; ZAP 70

Indexed keywords

ADAPTOR PROTEIN; BCR ABL PROTEIN; DOCKING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; HEMATOPOIETIC PROGENITOR KINASE 1; ONCOPROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTRANSFERASE; PROTEIN; PROTEIN CRK; PROTEIN P85; PROTEIN P97; SOS PROTEIN; STAT5 PROTEIN; UNCLASSIFIED DRUG;

EID: 0345257729     PISSN: 0257277X     EISSN: None     Source Type: Journal    
DOI: 10.1385/IR:28:2:79     Document Type: Review
Times cited : (15)

References (89)
  • 1
    • 0023864050 scopus 로고
    • A novel viral oncogene with structural similarity to phospholipase C
    • Mayer BJ, Hamaguchi M, Hanafusa H: A novel viral oncogene with structural similarity to phospholipase C. Nature 1988;332:272-275.
    • (1988) Nature , vol.332 , pp. 272-275
    • Mayer, B.J.1    Hamaguchi, M.2    Hanafusa, H.3
  • 2
    • 0026686182 scopus 로고
    • Two species of human CRK cDNA encode proteins with distinct biological activities
    • Matsuda M, Tanaka S, Nagata S, Kojima A, Kurata T, Shibuya M: Two species of human CRK cDNA encode proteins with distinct biological activities. Mol Cell Biol 1992;12:3482-3489.
    • (1992) Mol Cell Biol , vol.12 , pp. 3482-3489
    • Matsuda, M.1    Tanaka, S.2    Nagata, S.3    Kojima, A.4    Kurata, T.5    Shibuya, M.6
  • 3
    • 0026895954 scopus 로고
    • The product of the cellular crk gene consists primarily of SH2 and SH3 regions
    • Reichman CT, Mayer BJ, Keshav S, Hanafusa H: The product of the cellular crk gene consists primarily of SH2 and SH3 regions. Cell Growth Differ 1992;3:451-460.
    • (1992) Cell Growth Differ , vol.3 , pp. 451-460
    • Reichman, C.T.1    Mayer, B.J.2    Keshav, S.3    Hanafusa, H.4
  • 5
    • 0028335709 scopus 로고
    • The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells
    • Ogawa S, Toyoshima H, Kozutsumi H, Hagiwara K, Sakai R, Tanaka T, Hirano N, Mano H, Yazaki Y, Hirai H: The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells. Oncogene 1994;9: 1669-1678.
    • (1994) Oncogene , vol.9 , pp. 1669-1678
    • Ogawa, S.1    Toyoshima, H.2    Kozutsumi, H.3    Hagiwara, K.4    Sakai, R.5    Tanaka, T.6    Hirano, N.7    Mano, H.8    Yazaki, Y.9    Hirai, H.10
  • 6
    • 0027179910 scopus 로고
    • Isolation and chromosomal localization of CRKL, a human crk-like gene
    • ten Hoeve J, Morris C, Heisterkamp N, Groffen J: Isolation and chromosomal localization of CRKL, a human crk-like gene. Oncogene 1993;8:2469-2474.
    • (1993) Oncogene , vol.8 , pp. 2469-2474
    • Ten Hoeve, J.1    Morris, C.2    Heisterkamp, N.3    Groffen, J.4
  • 8
    • 0027940655 scopus 로고
    • SH2 and SH3 domains as molecular adhesives: The interactions of Crk and Abl
    • Feller SM, Ren R, Hanafusa H, Baltimore D: SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl. Trends Biochem Sec 1994;19:453-458.
    • (1994) Trends Biochem Sec , vol.19 , pp. 453-458
    • Feller, S.M.1    Ren, R.2    Hanafusa, H.3    Baltimore, D.4
  • 9
    • 0030180321 scopus 로고    scopus 로고
    • SH2 and SH3-containing adaptor proteins: Redundant or independent mediators of intracellular signal transduction
    • Birge RB, Knudsen BS, Besser D, Hanafusa H: SH2 and SH3-containing adaptor proteins: redundant or independent mediators of intracellular signal transduction. Genes Cells 1996;1:595-613.
    • (1996) Genes Cells , vol.1 , pp. 595-613
    • Birge, R.B.1    Knudsen, B.S.2    Besser, D.3    Hanafusa, H.4
  • 11
    • 0031946385 scopus 로고    scopus 로고
    • Role of the adapter protein CRKL in signal transduction of normal hematopoietic and BCR/ABL-transformed cells
    • Sattler M, Salgia R: Role of the adapter protein CRKL in signal transduction of normal hematopoietic and BCR/ABL-transformed cells. Leukemia 1998;12:637-644.
    • (1998) Leukemia , vol.12 , pp. 637-644
    • Sattler, M.1    Salgia, R.2
  • 13
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors-signalling complex formation and biological roles
    • Feller SM: Crk family adaptors-signalling complex formation and biological roles. Oncogene 2001;20: 6348-6371.
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.M.1
  • 14
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang Z, Shoelson SE, Chaudhuri M, et al.: SH2 domains recognize specific phosphopeptide sequences. Cell 1993;72:767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Shoelson, S.E.2    Chaudhuri, M.3
  • 15
    • 0035965340 scopus 로고    scopus 로고
    • T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein
    • Gelkop S, Babichev Y, Isakov N: T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein. J Biol Chem 2001;276:36,174-36,182.
    • (2001) J Biol Chem , vol.276 , pp. 36174-36182
    • Gelkop, S.1    Babichev, Y.2    Isakov, N.3
  • 16
    • 0033618287 scopus 로고    scopus 로고
    • T cell activation stimulates the association of enzymatically active tyrosine-phosphorylated ZAP-70 with the Crk adapter proteins
    • Gelkop S, Isakov N: T cell activation stimulates the association of enzymatically active tyrosine-phosphorylated ZAP-70 with the Crk adapter proteins. J Biol Chem 1999;274:21,519-21,527.
    • (1999) J Biol Chem , vol.274 , pp. 21519-21527
    • Gelkop, S.1    Isakov, N.2
  • 17
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
    • Knudsen BS, Feller SM, Hanafusa H: Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk. J Biol Chem 1994;269: 32,781-32,787.
    • (1994) J Biol Chem , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 20
    • 0029643950 scopus 로고
    • Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk
    • Wu X, Knudsen B, Feller SM, Zheng J, Sali A, Cowburn D, Hanafusa H, Kuriyan J: Structural basis for the specific interaction of lysine-containing proline-rich peptides with the N-terminal SH3 domain of c-Crk. Structure 1995;3:215-226.
    • (1995) Structure , vol.3 , pp. 215-226
    • Wu, X.1    Knudsen, B.2    Feller, S.M.3    Zheng, J.4    Sali, A.5    Cowburn, D.6    Hanafusa, H.7    Kuriyan, J.8
  • 22
    • 0028243505 scopus 로고
    • c-Abl kinase regulates the protein binding activity of c-Crk
    • Feller SM, Knudsen B, Hanafusa H: c-Abl kinase regulates the protein binding activity of c-Crk. EMBO J 1994;13:2341-2351.
    • (1994) EMBO J , vol.13 , pp. 2341-2351
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 23
    • 0031040941 scopus 로고    scopus 로고
    • Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site
    • de Jong R, ten Hoeve J, Heisterkamp N, Groffen J: Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site. Oncogene 1997;14:507-513.
    • (1997) Oncogene , vol.14 , pp. 507-513
    • De Jong, R.1    Ten Hoeve, J.2    Heisterkamp, N.3    Groffen, J.4
  • 24
    • 0028916892 scopus 로고
    • Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein
    • Rosen MK, Yamazaki T, Gish GD, Kay CM, Pawson T, Kay LE: Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature 1995;374:477-479.
    • (1995) Nature , vol.374 , pp. 477-479
    • Rosen, M.K.1    Yamazaki, T.2    Gish, G.D.3    Kay, C.M.4    Pawson, T.5    Kay, L.E.6
  • 25
    • 0029813117 scopus 로고    scopus 로고
    • A potential SH3 domain-binding site in the Crk SH2 domain
    • Anafi M, Rosen MK, Gish GD, Kay LE, Pawson T: A potential SH3 domain-binding site in the Crk SH2 domain. J Biol Chem 1996;271:21,365-21,374.
    • (1996) J Biol Chem , vol.271 , pp. 21365-21374
    • Anafi, M.1    Rosen, M.K.2    Gish, G.D.3    Kay, L.E.4    Pawson, T.5
  • 26
    • 0028122971 scopus 로고
    • CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells
    • Matsuda M, Hashimoto Y, Muroya K, Hasegawa H, Kurata T, Tanaka S, Nakamura S, Hattori S: CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells. Mol Cell Biol 1994;14:5495-5500.
    • (1994) Mol Cell Biol , vol.14 , pp. 5495-5500
    • Matsuda, M.1    Hashimoto, Y.2    Muroya, K.3    Hasegawa, H.4    Kurata, T.5    Tanaka, S.6    Nakamura, S.7    Hattori, S.8
  • 28
    • 0029928127 scopus 로고    scopus 로고
    • Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors
    • Smit L, van der Horst G, Borst J: Sos, Vav, and C3G participate in B cell receptor-induced signaling pathways and differentially associate with Shc-Grb2, Crk, and Crk-L adaptors. J Biol Chem 1996;271:8564-8569.
    • (1996) J Biol Chem , vol.271 , pp. 8564-8569
    • Smit, L.1    Van Der Horst, G.2    Borst, J.3
  • 29
    • 0033604512 scopus 로고    scopus 로고
    • Ras and Rap1: Two highly related small GTPases with distinct function
    • Zwartkruis FJ, Bos JL: Ras and Rap1: two highly related small GTPases with distinct function. Exp Cell Res 1999;253:157-165.
    • (1999) Exp Cell Res , vol.253 , pp. 157-165
    • Zwartkruis, F.J.1    Bos, J.L.2
  • 30
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy: Blocking of IL-2 gene transcription by activated Rap1
    • Boussiotis VA, Freeman GJ, Berezovskaya A, Barber DL, Nadler LM: Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1. Science 1997;278:124-128.
    • (1997) Science , vol.278 , pp. 124-128
    • Boussiotis, V.A.1    Freeman, G.J.2    Berezovskaya, A.3    Barber, D.L.4    Nadler, L.M.5
  • 31
    • 0033789882 scopus 로고    scopus 로고
    • Activation of the Ras-related GTPase Rap1 by thymocyte TCR engagement and during selection
    • Amsen D, Kruisbeek A, Bos JL, Reedquist K: Activation of the Ras-related GTPase Rap1 by thymocyte TCR engagement and during selection. Eur J Immunol 2000;30:2832-2841.
    • (2000) Eur J Immunol , vol.30 , pp. 2832-2841
    • Amsen, D.1    Kruisbeek, A.2    Bos, J.L.3    Reedquist, K.4
  • 32
    • 0033521637 scopus 로고    scopus 로고
    • Activation of the Drosophila C3G leads to cell fate changes and overproliferation during development, mediated by the RAS-MAPK pathway and RAP1
    • Ishimaru S, Williams R, Clark E, Hanafusa H, Gaul U: Activation of the Drosophila C3G leads to cell fate changes and overproliferation during development, mediated by the RAS-MAPK pathway and RAP1. EMBO J 1999;18:145-155.
    • (1999) EMBO J , vol.18 , pp. 145-155
    • Ishimaru, S.1    Williams, R.2    Clark, E.3    Hanafusa, H.4    Gaul, U.5
  • 33
    • 0032531756 scopus 로고    scopus 로고
    • Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling
    • Zwartkruis FJ, Wolthuis RM, Nabben NM, Franke B, Bos JL: Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling. EMBO J 1998;17:5905-5912.
    • (1998) EMBO J , vol.17 , pp. 5905-5912
    • Zwartkruis, F.J.1    Wolthuis, R.M.2    Nabben, N.M.3    Franke, B.4    Bos, J.L.5
  • 35
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • Reedquist KA, Fukazawa T, Panchamoorthy G, Langdon WY, Shoelson SE, Druker BJ, Band H: Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. J Biol Chem 1996:271:8435-8442.
    • (1996) J Biol Chem , vol.271 , pp. 8435-8442
    • Reedquist, K.A.1    Fukazawa, T.2    Panchamoorthy, G.3    Langdon, W.Y.4    Shoelson, S.E.5    Druker, B.J.6    Band, H.7
  • 36
    • 0033152359 scopus 로고    scopus 로고
    • CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G
    • Arai A, Nosaka Y, Kohsaka H, Miyasaka N, Miura O: CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G. Blood 1999;93:3713-3722.
    • (1999) Blood , vol.93 , pp. 3713-3722
    • Arai, A.1    Nosaka, Y.2    Kohsaka, H.3    Miyasaka, N.4    Miura, O.5
  • 37
    • 0033519691 scopus 로고    scopus 로고
    • Involvement of the adapter protein CRKL in integrin-mediated adhesion
    • Uemura N, Salgia R, Ewaniuk DS, Little MT, Griffin JD: Involvement of the adapter protein CRKL in integrin-mediated adhesion. Oncogene 1999;18:3343-3353.
    • (1999) Oncogene , vol.18 , pp. 3343-3353
    • Uemura, N.1    Salgia, R.2    Ewaniuk, D.S.3    Little, M.T.4    Griffin, J.D.5
  • 38
    • 0036371220 scopus 로고    scopus 로고
    • Abl: Mechanisms of regulation and activation
    • Smith JM, Mayer BJ: Abl: mechanisms of regulation and activation. Front Biosci 2002;7:d31-d42.
    • (2002) Front Biosci , vol.7
    • Smith, J.M.1    Mayer, B.J.2
  • 39
    • 0035342380 scopus 로고    scopus 로고
    • The role of the tyrosine kinase inhibitor STI571 in the treatment of cancer
    • ODwyer ME, Druker BJ: The role of the tyrosine kinase inhibitor STI571 in the treatment of cancer. Curr Cancer Drug Targets 2001;1:49-57.
    • (2001) Curr Cancer Drug Targets , vol.1 , pp. 49-57
    • ODwyer, M.E.1    Druker, B.J.2
  • 41
    • 0032930551 scopus 로고    scopus 로고
    • Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase
    • Ling P, Yao Z, Meyer CF, Wang XS, Oehrl W, Feller SM, Tan TH: Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase. Mol Cell Biol 1999;19:1359-1368.
    • (1999) Mol Cell Biol , vol.19 , pp. 1359-1368
    • Ling, P.1    Yao, Z.2    Meyer, C.F.3    Wang, X.S.4    Oehrl, W.5    Feller, S.M.6    Tan, T.H.7
  • 43
    • 0032512824 scopus 로고    scopus 로고
    • Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells
    • Gesbert F, Garbay C, Bertoglio J: Interleukin-2 stimulation induces tyrosine phosphorylation of p120-Cbl and CrkL and formation of multimolecular signaling complexes in T lymphocytes and natural killer cells. J Biol Chem 1998;273:3986-3993.
    • (1998) J Biol Chem , vol.273 , pp. 3986-3993
    • Gesbert, F.1    Garbay, C.2    Bertoglio, J.3
  • 44
    • 17544365654 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Cbl upon epidermal growth factor (EGF) stimulation and its association with EGF receptor and downstream signaling proteins
    • Fukazawa T, Miyake S, Band V, Band H: Tyrosine phosphorylation of Cbl upon epidermal growth factor (EGF) stimulation and its association with EGF receptor and downstream signaling proteins. J Biol Chem 1996;271: 14,554-14,559.
    • (1996) J Biol Chem , vol.271 , pp. 14554-14559
    • Fukazawa, T.1    Miyake, S.2    Band, V.3    Band, H.4
  • 45
    • 0030960106 scopus 로고    scopus 로고
    • CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2
    • Husson H, Mograbi B, Schmid-Antomarchi H, Fischer S, Rossi B: CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2. Oncogene 1997;14: 2331-2338.
    • (1997) Oncogene , vol.14 , pp. 2331-2338
    • Husson, H.1    Mograbi, B.2    Schmid-Antomarchi, H.3    Fischer, S.4    Rossi, B.5
  • 47
    • 0025942245 scopus 로고
    • The zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein
    • Chan AC, Irving BA, Fraser JD, Weiss A: The zeta chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein. Proc Natl Acad Sci USA 1991;88:9166-9170.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9166-9170
    • Chan, A.C.1    Irving, B.A.2    Fraser, J.D.3    Weiss, A.4
  • 48
    • 0028595695 scopus 로고
    • The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav
    • Katzav S, Sutherland M, Packham G, Yi T, Weiss A: The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav. J Biol Chem 1994;269: 32,579-33,285.
    • (1994) J Biol Chem , vol.269 , pp. 32579-33285
    • Katzav, S.1    Sutherland, M.2    Packham, G.3    Yi, T.4    Weiss, A.5
  • 51
    • 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: Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase. Science 1994;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
  • 52
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier R, Brennan T, Li Q, McCormack C, Seed B: Membrane compartmentation is required for efficient T cell activation. Immunity 1998;8:723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 54
    • 0030996848 scopus 로고    scopus 로고
    • ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains
    • Huby RDJ, Iwashima M, Weiss A, Ley SC: ZAP-70 protein tyrosine kinase is constitutively targeted to the T cell cortex independently of its SH2 domains. J Cell Biol 1997;137:1639-1649.
    • (1997) J Cell Biol , vol.137 , pp. 1639-1649
    • Huby, R.D.J.1    Iwashima, M.2    Weiss, A.3    Ley, S.C.4
  • 55
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer BJ, Hirai H, Sakai R: Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr Biol 1995;5:296-305.
    • (1995) Curr Biol , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 56
    • 0028938721 scopus 로고
    • Catalytic specificity of protein-tyrosine kinases is critical for selective signaling
    • Songyang Z, Carraway KLI, Eck MJ, et al.: Catalytic specificity of protein-tyrosine kinases is critical for selective signaling. Nature 1995;373:536-539.
    • (1995) Nature , vol.373 , pp. 536-539
    • Songyang, Z.1    Carraway, K.L.I.2    Eck, M.J.3
  • 57
    • 0029895645 scopus 로고    scopus 로고
    • Purification and characterization of human ZAP-70 proteins tyrosine kinase from a baculovirus expression system
    • Isakov N, Wange RL, Watts JD, Aebersold R, Samelson LE: Purification and characterization of human ZAP-70 proteins tyrosine kinase from a baculovirus expression system. J Biol Chem 1996;271:15,753-15,761.
    • (1996) J Biol Chem , vol.271 , pp. 15753-15761
    • Isakov, N.1    Wange, R.L.2    Watts, J.D.3    Aebersold, R.4    Samelson, L.E.5
  • 58
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptations to regulate protein tyrosine kinases
    • Thien CB, Langdon WY: Cbl: many adaptations to regulate protein tyrosine kinases. Nat Rev Mol Cell Biol 2001;2:294-307.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 59
    • 0036499010 scopus 로고    scopus 로고
    • Cbl and Cbl-b in T-cell regulation
    • Liu YC, Gu H: Cbl and Cbl-b in T-cell regulation. Trends Immunol 2002;23:140-143.
    • (2002) Trends Immunol , vol.23 , pp. 140-143
    • Liu, Y.C.1    Gu, H.2
  • 60
    • 0030712944 scopus 로고    scopus 로고
    • Cbl-mediated regulation of T cell receptor-induced AP1 activation: Implications for activation via the Ras signaling pathway
    • Rellahan BL, Graham LJ, Stoica B, De-Bell KE, Bonvini E: Cbl-mediated regulation of T cell receptor-induced AP1 activation: implications for activation via the Ras signaling pathway. J Biol Chem 1997;272: 30,806-30,811.
    • (1997) J Biol Chem , vol.272 , pp. 30806-30811
    • Rellahan, B.L.1    Graham, L.J.2    Stoica, B.3    De-Bell, K.E.4    Bonvini, E.5
  • 61
    • 0034614386 scopus 로고    scopus 로고
    • The RING finger domain of Cbl is essential for negative regulation of the Syk tyrosine kinase
    • Ota S, Hazeki K, Rao N, Lupher ML Jr, Andoniou CE, Druker B, Band H: The RING finger domain of Cbl is essential for negative regulation of the Syk tyrosine kinase. J Biol Chem 2000;275:414-422.
    • (2000) J Biol Chem , vol.275 , pp. 414-422
    • Ota, S.1    Hazeki, K.2    Rao, N.3    Lupher Jr., M.L.4    Andoniou, C.E.5    Druker, B.6    Band, H.7
  • 62
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota Y, Samelson LE: The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science 1997;276:418-420.
    • (1997) Science , vol.276 , pp. 418-420
    • Ota, Y.1    Samelson, L.E.2
  • 63
    • 0347263933 scopus 로고    scopus 로고
    • The Cbl protooncoprotein: A negative regulator of immune receptor signal transduction
    • Lupher ML Jr, Rao N, Eck MJ, Band H: The Cbl protooncoprotein: a negative regulator of immune receptor signal transduction. Immunol Today 1999;20:375-382.
    • (1999) Immunol Today , vol.20 , pp. 375-382
    • Lupher Jr., M.L.1    Rao, N.2    Eck, M.J.3    Band, H.4
  • 65
    • 0033582458 scopus 로고    scopus 로고
    • Activation of nuclear factor of activated T cells-(NFAT) and activating protein 1 (AP-1) by oncogenic 70Z Cbl requires an intact phosphotyrosine binding domain but not Crk(L) or p85 phosphatidylinositol 3-kinase association
    • van Leeuwen JE, Paik PK, Samelson LE: Activation of nuclear factor of activated T cells-(NFAT) and activating protein 1 (AP-1) by oncogenic 70Z Cbl requires an intact phosphotyrosine binding domain but not Crk(L) or p85 phosphatidylinositol 3-kinase association. J Biol Chem 1999;274:5153-5162.
    • (1999) J Biol Chem , vol.274 , pp. 5153-5162
    • Van Leeuwen, J.E.1    Paik, P.K.2    Samelson, L.E.3
  • 66
    • 0033582462 scopus 로고    scopus 로고
    • Dual regulation of T cell receptor-mediated signaling by oncogenic Cbl mutant 70Z
    • Zhang Z, Elly C, Altman A, Liu YC: Dual regulation of T cell receptor-mediated signaling by oncogenic Cbl mutant 70Z. J Biol Chem 1999;274:4883-4889.
    • (1999) J Biol Chem , vol.274 , pp. 4883-4889
    • Zhang, Z.1    Elly, C.2    Altman, A.3    Liu, Y.C.4
  • 67
    • 0033521883 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation
    • Elly C, Witte S, Zhang Z, Rosnet O, Lipkowitz S, Altman A, Liu YC: Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation. Oncogene 1999;18:1147-1156.
    • (1999) Oncogene , vol.18 , pp. 1147-1156
    • Elly, C.1    Witte, S.2    Zhang, Z.3    Rosnet, O.4    Lipkowitz, S.5    Altman, A.6    Liu, Y.C.7
  • 68
    • 0029946242 scopus 로고    scopus 로고
    • The two major sites of cbl tyrosine phosphorylation in abl-transformed cells select the crkL SH2 domain
    • Andoniou CE, Thien CB, Langdon WY: The two major sites of cbl tyrosine phosphorylation in abl-transformed cells select the crkL SH2 domain. Oncogene 1996;12: 1981-1989.
    • (1996) Oncogene , vol.12 , pp. 1981-1989
    • Andoniou, C.E.1    Thien, C.B.2    Langdon, W.Y.3
  • 69
    • 0030614453 scopus 로고    scopus 로고
    • 2+-stimulated activation of nuclear factor of activated T cells by a constitutively active Cbl mutant in T cells
    • 2+-stimulated activation of nuclear factor of activated T cells by a constitutively active Cbl mutant in T cells. J Biol Chem 1997;272:168-173.
    • (1997) J Biol Chem , vol.272 , pp. 168-173
    • Liu, Y.-C.1    Elly, C.2    Langdon, W.Y.3    Altman, A.4
  • 70
    • 0033593322 scopus 로고    scopus 로고
    • Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase
    • Hunter S, Burton EA, Wu SC, Anderson SM: Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase. J Biol Chem 1999;274:2097-2106.
    • (1999) J Biol Chem , vol.274 , pp. 2097-2106
    • Hunter, S.1    Burton, E.A.2    Wu, S.C.3    Anderson, S.M.4
  • 71
    • 0027191192 scopus 로고
    • Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase
    • Booker GW, Gout I, Downing AK, Driscoll PC, Boyd J, Waterfield MD, Campbell ID: Solution structure and ligand-binding site of the SH3 domain of the p85α subunit of phosphatidylinositol 3-kinase. Cell 1993;73: 813-822.
    • (1993) Cell , vol.73 , pp. 813-822
    • Booker, G.W.1    Gout, I.2    Downing, A.K.3    Driscoll, P.C.4    Boyd, J.5    Waterfield, M.D.6    Campbell, I.D.7
  • 72
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2
    • Sparks AB, Rider JE, Hoffman NG, Fowlkes DM, Quillam LA, Kay BK: Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2. Proc Natl Acad Sci USA 1996;93:1540-1544.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quillam, L.A.5    Kay, B.K.6
  • 74
    • 0029117423 scopus 로고
    • Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl
    • Hartley D, Meisner H, Corvera S: Specific association of the beta isoform of the p85 subunit of phosphatidylinositol-3 kinase with the proto-oncogene c-cbl. J Biol Chem 1995;270:18,260-18,263.
    • (1995) J Biol Chem , vol.270 , pp. 18260-18263
    • Hartley, D.1    Meisner, H.2    Corvera, S.3
  • 75
    • 0034815998 scopus 로고    scopus 로고
    • L-selectin tyrosine phosphorylates Cbl and induces association of tyrosine-phosphorylated Cbl with CrkL and Grb2
    • Brenner B, Kadel S, Birle A, Linderkamp O: L-selectin tyrosine phosphorylates Cbl and induces association of tyrosine-phosphorylated Cbl with CrkL and Grb2. Biochem Biophys Res Commun 2001;282:41-47.
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 41-47
    • Brenner, B.1    Kadel, S.2    Birle, A.3    Linderkamp, O.4
  • 76
    • 0035242032 scopus 로고    scopus 로고
    • SHP2 and cbl participate in alpha-chemokine receptor CXCR4-mediated signaling pathways
    • Chernock RD, Cherla RP, Ganju RK: SHP2 and cbl participate in alpha-chemokine receptor CXCR4-mediated signaling pathways. Blood 2001;97:608-615.
    • (2001) Blood , vol.97 , pp. 608-615
    • Chernock, R.D.1    Cherla, R.P.2    Ganju, R.K.3
  • 77
    • 0033621446 scopus 로고    scopus 로고
    • The adapter protein CrkL links Cbl to C3G after integrin ligation and enhances cell migration
    • Uemura N, Griffin JD: The adapter protein CrkL links Cbl to C3G after integrin ligation and enhances cell migration. J Biol Chem 1999;274:37,525-37, 532.
    • (1999) J Biol Chem , vol.274 , pp. 37525-37532
    • Uemura, N.1    Griffin, J.D.2
  • 78
    • 0029904694 scopus 로고    scopus 로고
    • Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes
    • Minegishi M, Tachibana K, Sato T, Iwata S, Nojima Y, Morimoto C: Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes. J Exp Med 1996;184:1365-1375.
    • (1996) J Exp Med , vol.184 , pp. 1365-1375
    • Minegishi, M.1    Tachibana, K.2    Sato, T.3    Iwata, S.4    Nojima, Y.5    Morimoto, C.6
  • 79
    • 0030871349 scopus 로고    scopus 로고
    • Ligation of the T cell antigen receptor induces tyrosine phosphorylation of p105CasL, a member of the p130Cas-related docking protein family, and its subsequent binding to the Src homology 2 domain of c-Crk
    • Kanda H, Mimura T, Morino N, Hamasaki K, Nakamoto T, Hirai H, Morimoto C, Yazaki Y, Nojima Y: Ligation of the T cell antigen receptor induces tyrosine phosphorylation of p105CasL, a member of the p130Cas-related docking protein family, and its subsequent binding to the Src homology 2 domain of c-Crk. Eur J Immunol 1997;27:2113-2117.
    • (1997) Eur J Immunol , vol.27 , pp. 2113-2117
    • Kanda, H.1    Mimura, T.2    Morino, N.3    Hamasaki, K.4    Nakamoto, T.5    Hirai, H.6    Morimoto, C.7    Yazaki, Y.8    Nojima, Y.9
  • 80
    • 0032513128 scopus 로고    scopus 로고
    • T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G
    • Ohashi Y, Tachibana K, Kamiguchi K, Fujita H, Morimoto C: T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G. J Biol Chem 1998;273:6446-6451.
    • (1998) J Biol Chem , vol.273 , pp. 6446-6451
    • Ohashi, Y.1    Tachibana, K.2    Kamiguchi, K.3    Fujita, H.4    Morimoto, C.5
  • 81
  • 84
    • 0028836186 scopus 로고
    • Stimulation of NK-like YT cells via leukocyte function-associated antigen (LFA)-1. Possible involvement of LFA-1-associated tyrosine kinase in signal transduction after recognition of NK target cells
    • Sugie K, Minami Y, Kawakami T, Uchida A: Stimulation of NK-like YT cells via leukocyte function-associated antigen (LFA)-1. Possible involvement of LFA-1-associated tyrosine kinase in signal transduction after recognition of NK target cells. J Immunol 1995;154: 1691-1698.
    • (1995) J Immunol , vol.154 , pp. 1691-1698
    • Sugie, K.1    Minami, Y.2    Kawakami, T.3    Uchida, A.4
  • 85
    • 0032540957 scopus 로고    scopus 로고
    • A new tyrosine-phosphorylated 97-kDa adaptor protein mediates interleukin-2-induced association of SHP-2 with p85-phosphatidylinositol 3-kinase in human T lymphocytes
    • Gesbert F, Guenzi C, Bertoglio J: A new tyrosine-phosphorylated 97-kDa adaptor protein mediates interleukin-2-induced association of SHP-2 with p85-phosphatidylinositol 3-kinase in human T lymphocytes. J Biol Chem 1998;273:18,273-18,281.
    • (1998) J Biol Chem , vol.273 , pp. 18273-18281
    • Gesbert, F.1    Guenzi, C.2    Bertoglio, J.3
  • 86
    • 0030953218 scopus 로고    scopus 로고
    • Characterization of a novel tyrosine phosphorylated 100-kDa protein that binds to SHP-2 and phosphatidylinositol 3′-kinase in myeloid cells
    • Carlberg K, Rohrschneider LR: Characterization of a novel tyrosine phosphorylated 100-kDa protein that binds to SHP-2 and phosphatidylinositol 3′-kinase in myeloid cells. J Biol Chem 1997;272:15,943-15,950.
    • (1997) J Biol Chem , vol.272 , pp. 15943-15950
    • Carlberg, K.1    Rohrschneider, L.R.2
  • 87
    • 0030974476 scopus 로고    scopus 로고
    • Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells
    • Gu H, Griffin JD, Neel BG: Characterization of two SHP-2-associated binding proteins and potential substrates in hematopoietic cells. J Biol Chem 1997;272: 16,421-16,430.
    • (1997) J Biol Chem , vol.272 , pp. 16421-16430
    • Gu, H.1    Griffin, J.D.2    Neel, B.G.3
  • 88
    • 0030698073 scopus 로고    scopus 로고
    • Interleukin-3 induces association of the protein-tyrosine phosphatase SHP2 and phosphatidylinositol 3-kinase with a 100-kDa tyrosine-phosphorylated protein inhemopoietic cells
    • Craddock BL, Welham MJ: Interleukin-3 induces association of the protein-tyrosine phosphatase SHP2 and phosphatidylinositol 3-kinase with a 100-kDa tyrosine-phosphorylated protein inhemopoietic cells. J Biol Chem 1997;272:29,281-29,289.
    • (1997) J Biol Chem , vol.272 , pp. 29281-29289
    • Craddock, B.L.1    Welham, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.