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Volumn 20, Issue 4, 2008, Pages 485-497

Dual role of Cbl links critical events in BCR endocytosis

Author keywords

Capping; Crk; Cytoskeleton; Rac

Indexed keywords

B LYMPHOCYTE RECEPTOR; CBL PROTEIN; PROTEIN CRKII; RAC PROTEIN; REGULATOR PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 41149152423     PISSN: 09538178     EISSN: 14602377     Source Type: Journal    
DOI: 10.1093/intimm/dxn010     Document Type: Article
Times cited : (18)

References (62)
  • 1
    • 0033828928 scopus 로고    scopus 로고
    • The ins and outs of getting in: Structures and signals that enhance BCR or Fc receptor-mediated antigen presentation
    • Shen, L., Lang, M. L. and Wade, W. F. 2002. The ins and outs of getting in: Structures and signals that enhance BCR or Fc receptor-mediated antigen presentation. Immunopharmacology. 49:227.
    • (2002) Immunopharmacology , vol.49 , pp. 227
    • Shen, L.1    Lang, M.L.2    Wade, W.F.3
  • 2
    • 0035143661 scopus 로고    scopus 로고
    • The control and facilitation of MHC class II antigen processing by the BCR
    • Siemasko, K. and Clark, M. R. 2001. The control and facilitation of MHC class II antigen processing by the BCR. Curr. Opin. Immunol. 13:32.
    • (2001) Curr. Opin. Immunol , vol.13 , pp. 32
    • Siemasko, K.1    Clark, M.R.2
  • 3
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Watts, C. 1997. Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15:821.
    • (1997) Annu. Rev. Immunol , vol.15 , pp. 821
    • Watts, C.1
  • 4
  • 5
    • 0035003212 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton by Rho-family GTPases: Implications for tumour cell invasion
    • Price, L. S. and Collard, J. G. 2001. Regulation of the cytoskeleton by Rho-family GTPases: Implications for tumour cell invasion. Semin. Cancer Biol. 11:167.
    • (2001) Semin. Cancer Biol , vol.11 , pp. 167
    • Price, L.S.1    Collard, J.G.2
  • 6
    • 0033180472 scopus 로고    scopus 로고
    • Endocytosis and mitogenic signaling
    • DiFore, P. P. and Gill, G. N. 1999. Endocytosis and mitogenic signaling. Curr. Opin. Cell Biol. 11:483.
    • (1999) Curr. Opin. Cell Biol , vol.11 , pp. 483
    • DiFore, P.P.1    Gill, G.N.2
  • 9
    • 0030889218 scopus 로고    scopus 로고
    • The product of the proto-oncogene c-cbl: A negative regulator of the Syk tyrosine kinase
    • Ota, Y. and Samelson, L. 1997. The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase. Science. 276:418.
    • (1997) Science , vol.276 , pp. 418
    • Ota, Y.1    Samelson, L.2
  • 11
    • 0029876948 scopus 로고    scopus 로고
    • 996. Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • Reedquist, K. A., Fukazawa, T., Panchamoorthy, G. et al. 996. Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. J. Biol. Chem. 271:8435.
    • J. Biol. Chem , vol.271 , pp. 8435
    • Reedquist, K.A.1    Fukazawa, T.2    Panchamoorthy, G.3
  • 12
    • 0029664998 scopus 로고    scopus 로고
    • Interaction of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation
    • Buday, L., Khwaja, A., Sipeki, S., Farago, A. and Downward, J. 1996. Interaction of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation. J. Biol. Chem. 271:6159.
    • (1996) J. Biol. Chem , vol.271 , pp. 6159
    • Buday, L.1    Khwaja, A.2    Sipeki, S.3    Farago, A.4    Downward, J.5
  • 13
    • 0029655999 scopus 로고    scopus 로고
    • The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner
    • Ribon, V., Hubbell, S., Herrera, R. and Saltiel, A. R. 1996. The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner. Mol. Cell. Biol. 16:45.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 45
    • Ribon, V.1    Hubbell, S.2    Herrera, R.3    Saltiel, A.R.4
  • 14
    • 0029831323 scopus 로고    scopus 로고
    • Formation of Shc/Grb2- and Crk adaptor complexes containing tyrosine phosphorylated Cbl upon stimulation of the B-cell antigen receptor
    • Smit, L., van der Horst, G. and Borst, G. 1996. Formation of Shc/Grb2- and Crk adaptor complexes containing tyrosine phosphorylated Cbl upon stimulation of the B-cell antigen receptor. Oncogene. 13:381.
    • (1996) Oncogene , vol.13 , pp. 381
    • Smit, L.1    van der Horst, G.2    Borst, G.3
  • 15
    • 0030070343 scopus 로고    scopus 로고
    • Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes
    • Fournel, M., Davidson, D., Weil, R. and Veillette, A. 1996. Association of tyrosine protein kinase Zap-70 with the protooncogene product p120c-cbl in T lymphocytes. J. Exp. Med. 183:301.
    • (1996) J. Exp. Med , vol.183 , pp. 301
    • Fournel, M.1    Davidson, D.2    Weil, R.3    Veillette, A.4
  • 16
    • 0029098389 scopus 로고
    • The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase
    • Cory, G. O., Lovering, R. C., Hinshelwood, S., MacCarthy-Morrogh, L., Levinsky, R. J. and Kinnon, C. 1995. The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase. J. Exp. Med. 182:611.
    • (1995) J. Exp. Med , vol.182 , pp. 611
    • Cory, G.O.1    Lovering, R.C.2    Hinshelwood, S.3    MacCarthy-Morrogh, L.4    Levinsky, R.J.5    Kinnon, C.6
  • 17
    • 28844490931 scopus 로고    scopus 로고
    • The Cbl interactome and its function
    • Schmidt, M. H. H. and Dikic, I. 2005. The Cbl interactome and its function. Mol. Cell. Biol. 6:907.
    • (2005) Mol. Cell. Biol , vol.6 , pp. 907
    • Schmidt, M.H.H.1    Dikic, I.2
  • 18
    • 0035106341 scopus 로고    scopus 로고
    • Ring finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation
    • Thien, C. B., Walker, F. and Langdon, W. Y. 2001. Ring finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation. Mol. Cell. 7:355.
    • (2001) Mol. Cell , vol.7 , pp. 355
    • Thien, C.B.1    Walker, F.2    Langdon, W.Y.3
  • 19
    • 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. et al. 2000. The ring finger domain of Cbl is essential for negative regulation of the Syk tyrosine kinase. J. Biol. Chem. 275:414.
    • (2000) J. Biol. Chem , vol.275 , pp. 414
    • Ota, S.1    Hazeki, K.2    Rao, N.3
  • 20
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl ring finger and UbcH7
    • Yokouchi, M., Kondo, T., Houghton, A. et al. 1999. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl ring finger and UbcH7. J. Biol. Chem. 274:21707.
    • (1999) J. Biol. Chem , vol.274 , pp. 21707
    • Yokouchi, M.1    Kondo, T.2    Houghton, A.3
  • 21
    • 0033529537 scopus 로고    scopus 로고
    • The ring finger of c-Cbl mediates desensitization of the epidermal growth factor receptor
    • Waterman, H., Levkowitz, G., Alroy, I. and Yarden, Y. 1999. The ring finger of c-Cbl mediates desensitization of the epidermal growth factor receptor. J. Biol. Chem. 274:22151.
    • (1999) J. Biol. Chem , vol.274 , pp. 22151
    • Waterman, H.1    Levkowitz, G.2    Alroy, I.3    Yarden, Y.4
  • 22
    • 0033169024 scopus 로고    scopus 로고
    • The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation
    • Lee, P. S., Wang, Y., Dominguez, M. G. et al. 1999. The Cbl protooncoprotein stimulates CSF-1 receptor multiubiquitination and endocytosis, and attenuates macrophage proliferation. EMBO J. 18:3616.
    • (1999) EMBO J , vol.18 , pp. 3616
    • Lee, P.S.1    Wang, Y.2    Dominguez, M.G.3
  • 23
    • 0032217156 scopus 로고    scopus 로고
    • C-Cbl/SLI-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor
    • Levkowitz, G., Waterman, H., Zamir, E. et al. 1998. C-Cbl/SLI-1 regulates endocytic sorting and ubiquitination of the epidermal growth factor receptor. Genes Dev. 12:3663.
    • (1998) Genes Dev , vol.12 , pp. 3663
    • Levkowitz, G.1    Waterman, H.2    Zamir, E.3
  • 24
    • 0032493444 scopus 로고    scopus 로고
    • The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha
    • Miyake, S., Lupher, M. L. Jr, Druker, B. and Band, H. 1998. The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha. Proc. Natl Acad. Sci. USA. 95:7927.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7927
    • Miyake, S.1    Lupher Jr, M.L.2    Druker, B.3    Band, H.4
  • 25
    • 6344262249 scopus 로고    scopus 로고
    • Differential regulation of the B cell receptor-mediated signalling by the E3 ubiquitin ligase Cbl
    • Shao, Y., Yang, C., Elly, C. and Liu, Y. C. 2004. Differential regulation of the B cell receptor-mediated signalling by the E3 ubiquitin ligase Cbl. J. Biol. Chem. 279:43646.
    • (2004) J. Biol. Chem , vol.279 , pp. 43646
    • Shao, Y.1    Yang, C.2    Elly, C.3    Liu, Y.C.4
  • 26
    • 0037944241 scopus 로고    scopus 로고
    • Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through uniquitination of the tyrosine kinase Syk
    • Sohn, H. W., Gu, H. and Pierce, S. K. 2003. Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through uniquitination of the tyrosine kinase Syk. J. Exp. Med. 197:1511.
    • (2003) J. Exp. Med , vol.197 , pp. 1511
    • Sohn, H.W.1    Gu, H.2    Pierce, S.K.3
  • 27
    • 0029671073 scopus 로고    scopus 로고
    • p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase
    • Panchamoorthy, G., Fukazawa, T., Miyake, S. et al. 1996. p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 271:3187.
    • (1996) J. Biol. Chem , vol.271 , pp. 3187
    • Panchamoorthy, G.1    Fukazawa, T.2    Miyake, S.3
  • 28
    • 33845324847 scopus 로고    scopus 로고
    • Src-like adaptor protein (SLAP) regulates B cell receptor levels in a c-Cbl-dependent manner
    • Dragone, L. L., Myers, M. D., White, C. et al. 2006. Src-like adaptor protein (SLAP) regulates B cell receptor levels in a c-Cbl-dependent manner. Proc. Natl Acad. Sci. 103:19202.
    • (2006) Proc. Natl Acad. Sci , vol.103 , pp. 19202
    • Dragone, L.L.1    Myers, M.D.2    White, C.3
  • 29
    • 0037126634 scopus 로고    scopus 로고
    • The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation
    • Rao, N., Ghosh, A. K., Ota, S. et al. 2001. The non-receptor tyrosine kinase Syk is a target of Cbl-mediated ubiquitylation upon B-cell receptor stimulation. EMBO J. 20:7085.
    • (2001) EMBO J , vol.20 , pp. 7085
    • Rao, N.1    Ghosh, A.K.2    Ota, S.3
  • 30
    • 0030875967 scopus 로고    scopus 로고
    • Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathways in B cells
    • Li, H.-L., Forman, M. S., Kurosaki, T. and Puré, E. 1997. Syk is required for BCR-mediated activation of p90Rsk, but not p70S6k, via a mitogen-activated protein kinase-independent pathways in B cells. J. Biol. Chem. 272:18200.
    • (1997) J. Biol. Chem , vol.272 , pp. 18200
    • Li, H.-L.1    Forman, M.S.2    Kurosaki, T.3    Puré, E.4
  • 31
    • 0028180858 scopus 로고
    • Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways
    • Takata, M., Sabe, H., Hata, A. et al. 1994. Tyrosine kinases Lyn and Syk regulate B cell receptor-coupled Ca2+ mobilization through distinct pathways. EMBO J. 13:1341.
    • (1994) EMBO J , vol.13 , pp. 1341
    • Takata, M.1    Sabe, H.2    Hata, A.3
  • 32
    • 0034695890 scopus 로고    scopus 로고
    • Cbl suppresses B Cell Receptor-mediated phospholipase C (PLC)-γ2 activation by regulating B Cell Linker protein-PLC-γ2 binding
    • Yasuda, T., Maeda, A., Kurosaki, M. et al. 2000. Cbl suppresses B Cell Receptor-mediated phospholipase C (PLC)-γ2 activation by regulating B Cell Linker protein-PLC-γ2 binding. J. Exp. Med. 191:641.
    • (2000) J. Exp. Med , vol.191 , pp. 641
    • Yasuda, T.1    Maeda, A.2    Kurosaki, M.3
  • 33
    • 0036911112 scopus 로고    scopus 로고
    • c-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-regulation
    • Namamura, M., Jang, I. K., Kole, H., Huang, F., Haines, D. and Gu, H. 2002. c-Cbl and Cbl-b regulate T cell responsiveness by promoting ligand-induced TCR down-regulation. Nat. Immunol. 3:1192.
    • (2002) Nat. Immunol , vol.3 , pp. 1192
    • Namamura, M.1    Jang, I.K.2    Kole, H.3    Huang, F.4    Haines, D.5    Gu, H.6
  • 34
    • 0037124330 scopus 로고    scopus 로고
    • Constitutive endocytosis and degradation of the pre-T cell receptor
    • Panigada, M., Porcellini, S., Barbier, E. et al. 2002. Constitutive endocytosis and degradation of the pre-T cell receptor. J. Exp. Med. 195:1585.
    • (2002) J. Exp. Med , vol.195 , pp. 1585
    • Panigada, M.1    Porcellini, S.2    Barbier, E.3
  • 35
    • 23844475373 scopus 로고    scopus 로고
    • Selective defect in antigen-induced TCR internalization at the immune synapse of CD8 T cells bearing the ZAP-70(Y282F) mutation
    • Davanture, S., Leignadier, J., Milani, P. et al. 2005. Selective defect in antigen-induced TCR internalization at the immune synapse of CD8 T cells bearing the ZAP-70(Y282F) mutation. J. Immunol. 175:3140.
    • (2005) J. Immunol , vol.175 , pp. 3140
    • Davanture, S.1    Leignadier, J.2    Milani, P.3
  • 36
    • 0028237972 scopus 로고
    • Purification and identification of tyrosine-phosphorylated proteins from B lymphocytes stimulated through the antigen receptor
    • Gold, M. R., Yungwirth, T., Sutherland, C. L. et al. 1994. Purification and identification of tyrosine-phosphorylated proteins from B lymphocytes stimulated through the antigen receptor. Electrophoresis. 15:441.
    • (1994) Electrophoresis , vol.15 , pp. 441
    • Gold, M.R.1    Yungwirth, T.2    Sutherland, C.L.3
  • 37
    • 0026572982 scopus 로고
    • Tyrosine phosphorylation is required for ligand-induced internalization of the antigen receptor on B lymphocytes
    • Puré, E. and Tardelli, L. 1992. Tyrosine phosphorylation is required for ligand-induced internalization of the antigen receptor on B lymphocytes. Proc. Natl Acad. Sci. USA. 89:114.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 114
    • Puré, E.1    Tardelli, L.2
  • 38
    • 12044256844 scopus 로고
    • Tumour induction by activated abl involves tyrosine phosphorylation of the product of the cbl oncogene
    • Andoniou, C. E., Thien, C. B. F. and Langdon, W. Y. 1994. Tumour induction by activated abl involves tyrosine phosphorylation of the product of the cbl oncogene. EMBO J. 13:4515.
    • (1994) EMBO J , vol.13 , pp. 4515
    • Andoniou, C.E.1    Thien, C.B.F.2    Langdon, W.Y.3
  • 39
    • 34248512113 scopus 로고    scopus 로고
    • Control of the B cell-intrinsic tolerance programs by ubiquitin ligases Cbl and Cbl-b
    • Kitaura, Y., Jang, I. K., Wang, Y. et al. 2007. Control of the B cell-intrinsic tolerance programs by ubiquitin ligases Cbl and Cbl-b. Immunity. 26:567.
    • (2007) Immunity , vol.26 , pp. 567
    • Kitaura, Y.1    Jang, I.K.2    Wang, Y.3
  • 40
    • 41149165277 scopus 로고    scopus 로고
    • c-Cbl-facilitated cytoskeletal effects in vAbl-transformed fibroblasts are regulated by membrane association of c-Cbl
    • Swaminathan, G., Feschenko, E. A. and Tsygankov, A. Y. 2007. c-Cbl-facilitated cytoskeletal effects in vAbl-transformed fibroblasts are regulated by membrane association of c-Cbl. Oncogene. 1:1.
    • (2007) Oncogene , vol.1 , pp. 1
    • Swaminathan, G.1    Feschenko, E.A.2    Tsygankov, A.Y.3
  • 41
    • 3042730952 scopus 로고    scopus 로고
    • Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites
    • Haglund, K., Ivankovic-Dikic, I., Shimokawa, N., Kruh, G. D. and Dikic, I. 2004. Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites. J. Cell Sci. 117:2557.
    • (2004) J. Cell Sci , vol.117 , pp. 2557
    • Haglund, K.1    Ivankovic-Dikic, I.2    Shimokawa, N.3    Kruh, G.D.4    Dikic, I.5
  • 42
    • 0344824500 scopus 로고    scopus 로고
    • Rapid microtubule-dependent induction of neurite-like extensions in NIH 3T3 fibroblasts by inhibition of RACK and Cbl
    • Scaife, R. M., Job, D. and Langdon, W. Y. 2003. Rapid microtubule-dependent induction of neurite-like extensions in NIH 3T3 fibroblasts by inhibition of RACK and Cbl. Mol. Biol. Cell. 14:4605.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4605
    • Scaife, R.M.1    Job, D.2    Langdon, W.Y.3
  • 43
    • 0035825121 scopus 로고    scopus 로고
    • Cbl associates with Pyk2 and Src to regulate Src kinase activity, αvβ3 integrin-mediated signaling, cell adhesion, and osteoclasts motility
    • Sanjay, A., Houghton, A., Neff, L. et al. 2001. Cbl associates with Pyk2 and Src to regulate Src kinase activity, αvβ3 integrin-mediated signaling, cell adhesion, and osteoclasts motility. J. Cell Biol. 152:181.
    • (2001) J. Cell Biol , vol.152 , pp. 181
    • Sanjay, A.1    Houghton, A.2    Neff, L.3
  • 45
    • 0037009371 scopus 로고    scopus 로고
    • Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling
    • Abassi, Y. A. and Vuori, K. 2002. Tyrosine 221 in Crk regulates adhesion-dependent membrane localization of Crk and Rac and activation of Rac signaling. EMBO J. 21:4571.
    • (2002) EMBO J , vol.21 , pp. 4571
    • Abassi, Y.A.1    Vuori, K.2
  • 46
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho, S. Y. and Klemke, R. L. 2002. Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J. Cell Biol. 156:725.
    • (2002) J. Cell Biol , vol.156 , pp. 725
    • Cho, S.Y.1    Klemke, R.L.2
  • 47
    • 0033771902 scopus 로고    scopus 로고
    • CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Ceanorhabditis elegans
    • Reddien, P. W. and Horvitz, H. R. 2000. CED-2/CrkII and CED-10/Rac control phagocytosis and cell migration in Ceanorhabditis elegans. Nat. Cell Biol. 2:131.
    • (2000) Nat. Cell Biol , vol.2 , pp. 131
    • Reddien, P.W.1    Horvitz, H.R.2
  • 48
    • 0035477599 scopus 로고    scopus 로고
    • Deficiency of small GTPase Rac2 affects T cell activation
    • Yu, H., Leitenberg, D., Li, B. and Flavell, R. A. 2001. Deficiency of small GTPase Rac2 affects T cell activation. J. Exp. Med. 194:915.
    • (2001) J. Exp. Med , vol.194 , pp. 915
    • Yu, H.1    Leitenberg, D.2    Li, B.3    Flavell, R.A.4
  • 49
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors- signaling complex formation and biological roles
    • Feller, S. M. 2001. Crk family adaptors- signaling complex formation and biological roles. Oncogene. 20:6348.
    • (2001) Oncogene , vol.20 , pp. 6348
    • Feller, S.M.1
  • 50
    • 0029946242 scopus 로고
    • The two major sites of cbl tyrosine phosphorylation in abl-transformed cells select the crkL SH2 domain
    • Andoniou, C. E., Thien, C. B. F. and Langdon, W. Y. 1996. The two major sites of cbl tyrosine phosphorylation in abl-transformed cells select the crkL SH2 domain. Oncogene. 12:1981.
    • (1981) Oncogene , vol.12
    • Andoniou, C.E.1    Thien, C.B.F.2    Langdon, W.Y.3
  • 51
    • 0036645535 scopus 로고    scopus 로고
    • Cbl-b positively regulates Btk-mediated activation of phospholipase C-γ2 in B cells
    • Yasuda, T., Tezuka, T., Maeda, A. et al. 2002. Cbl-b positively regulates Btk-mediated activation of phospholipase C-γ2 in B cells. J. Exp. Med. 196:51.
    • (2002) J. Exp. Med , vol.196 , pp. 51
    • Yasuda, T.1    Tezuka, T.2    Maeda, A.3
  • 52
    • 0035811573 scopus 로고    scopus 로고
    • Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor
    • Miyoshi-Akiyama, T., Aleman, L. M., Smith, J. M., Adler, C. E. and Mayer, B. J. 2001. Regulation of Cbl phosphorylation by the Abl tyrosine kinase and the Nck SH2/SH3 adaptor. Oncogene. 20:4058.
    • (2001) Oncogene , vol.20 , pp. 4058
    • Miyoshi-Akiyama, T.1    Aleman, L.M.2    Smith, J.M.3    Adler, C.E.4    Mayer, B.J.5
  • 53
    • 0037326675 scopus 로고    scopus 로고
    • The multi-adaptor proto-oncoprotein Cbl is a key regulator of Rac and actin assembly
    • Scaife, R. M., Courtneidge, S. A. and Langdon, W. Y. 2002. The multi-adaptor proto-oncoprotein Cbl is a key regulator of Rac and actin assembly. J. Cell Sci. 116:463.
    • (2002) J. Cell Sci , vol.116 , pp. 463
    • Scaife, R.M.1    Courtneidge, S.A.2    Langdon, W.Y.3
  • 54
    • 0035193064 scopus 로고    scopus 로고
    • Visualization of negative signaling in B cells by quantitative confocal microscopy
    • Phee, H., Rodgers, W. and Coggeshall, K. M. 2001. Visualization of negative signaling in B cells by quantitative confocal microscopy. Mol. Cell. Biol. 21:8615.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 8615
    • Phee, H.1    Rodgers, W.2    Coggeshall, K.M.3
  • 55
    • 0942265527 scopus 로고    scopus 로고
    • Mechanisms of guanine nucleotide exchange and Rac-mediated signaling revealed by a dominant negative Trio mutant
    • Debreceni, B., Gao, Y., Gao, F., Zhu, K., Jia, B. and Zheng, Y. 2003. Mechanisms of guanine nucleotide exchange and Rac-mediated signaling revealed by a dominant negative Trio mutant. J. Biol. Chem. 279:3777.
    • (2003) J. Biol. Chem , vol.279 , pp. 3777
    • Debreceni, B.1    Gao, Y.2    Gao, F.3    Zhu, K.4    Jia, B.5    Zheng, Y.6
  • 56
    • 0037450822 scopus 로고    scopus 로고
    • A mouse with a loss-of-function mutation in the c-cbl TKB domain shows perturbed thymocyte signalling without enhancing the activity of the ZAP-70 tyrosine kinase
    • Thien, C. B. F., Scaife, R. M., Papadimitriou, J. M., Murphy, M. M., Bowtell, D. D. L. and Langdon, W. Y. 2003. A mouse with a loss-of-function mutation in the c-cbl TKB domain shows perturbed thymocyte signalling without enhancing the activity of the ZAP-70 tyrosine kinase. J. Exp. Med. 197:503.
    • (2003) J. Exp. Med , vol.197 , pp. 503
    • Thien, C.B.F.1    Scaife, R.M.2    Papadimitriou, J.M.3    Murphy, M.M.4    Bowtell, D.D.L.5    Langdon, W.Y.6
  • 57
    • 0031042152 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the product of the c-cbl protooncogene is induced after integrin stimulation
    • Manie, S. N., Sattler, M., Astier, A. et al. 1997. Tyrosine phosphorylation of the product of the c-cbl protooncogene is induced after integrin stimulation. Exp. Hematol. 25:45.
    • (1997) Exp. Hematol , vol.25 , pp. 45
    • Manie, S.N.1    Sattler, M.2    Astier, A.3
  • 58
    • 0141637441 scopus 로고    scopus 로고
    • Cbl signaling networks in the regulation of cell function
    • Dikic, I., Szymkiewicz, I. and Soubeyran, P. 2003. Cbl signaling networks in the regulation of cell function. Cell. Mol. Life Sci. 60:1805.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1805
    • Dikic, I.1    Szymkiewicz, I.2    Soubeyran, P.3
  • 59
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signaling to actin cytoskeletal dynamics
    • Edwards, D. C., Sanders, L. C., Bokoch, G. M. and Gill, C. N. 1999. Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signaling to actin cytoskeletal dynamics. Nat. Cell Biol. 1:115.
    • (1999) Nat. Cell Biol , vol.1 , pp. 115
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, C.N.4
  • 60
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., Higuchi, O., Ohashi, K. et al. 1998. Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature. 393:809.
    • (1998) Nature , vol.393 , pp. 809
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3
  • 61
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • Arber, S., Barbayannis, F. A., Hanser, H. et al. 1998. Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature. 393:739.
    • (1998) Nature , vol.393 , pp. 739
    • Arber, S.1    Barbayannis, F.A.2    Hanser, H.3
  • 62
    • 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. and Borst, J. 1996. 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. 271:8564.
    • (1996) J. Biol. Chem , vol.271 , pp. 8564
    • Smit, L.1    van der Horst, G.2    Borst, J.3


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