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• W2023561231 abstract "Engagement of the T-cell receptor (TCR)–CD3 complex induces a rapid increase in the activities of Src-family and Syk/Zap-70-family kinases [1Weiss A Littman DR Signal transduction by lymphocyte antigen receptors.Cell. 1994; 76: 263-274Abstract Full Text PDF PubMed Scopus (1932) Google Scholar, 2Wange RL Samelson LE Complex complexes: signaling at the TCR.Immunity. 1996; 5: 197-205Abstract Full Text Full Text PDF PubMed Scopus (457) Google Scholar]. These activated kinases then induce the tyrosine phosphorylation of multiple intracellular proteins, eventually leading to T-cell activation. One of the prominent substrates for these kinases is the adaptor protein Cbl [[3]Liu Y-C Altman A Cbl: complex formation and functional implications.Cell Signaling. 1998; 10: 377-385Crossref PubMed Scopus (84) Google Scholar] and recent studies suggest that Cbl negatively regulates upstream kinases such as Syk and Zap-70 [4Ota Y Samelson LE The product of the proto-oncogene c-Cbl: a negative regulator of the Syk tyrosine kinase.Science. 1997; 276: 418-420Crossref PubMed Scopus (225) Google Scholar, 5Murphy MA Schnall RG Venter DJ Barnett L Bertoncello I Thien CB et al.Tissue hyperplasia and enhanced T-cell signaling via Zap-70 in c-Cbl-deficient mice.Mol Cell Biol. 1998; 18: 4872-4882Crossref PubMed Scopus (329) Google Scholar]. Cbl-b, a homologue of Cbl, is widely expressed in many tissues and cells including hematopoietic cells [6Keane MM Rivero Lezcano OM Mitchell JA Robbins KC Lipkowitz S Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene.Oncogene. 1995; 10: 2367-2377PubMed Google Scholar, 7Bustelo XR Crespo P Lopez BM Gutkind JS Barbacid M Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav- mediated c-Jun N-terminal kinase activation.Oncogene. 1997; 15: 2511-2520Crossref PubMed Scopus (80) Google Scholar]. Cbl-b undergoes rapid tyrosine phosphorylation upon stimulation of the TCR and cytokine receptors [8Lavagna-Sevenier C Marhetto S Birnbaum D Rosnet O The Cbl-related protein Cblb participates in FLT3 and interleukin-7 receptor signal transduction in pro-B cells.J Biol Chem. 1998; 273: 14962-14967Crossref PubMed Scopus (48) Google Scholar, 9Elly C Zhang Z Rosnet O Lipokowitz S Altman A Liu Y-C Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation.Oncogene. 1999; 18: 1153-1162Crossref Scopus (53) Google Scholar]. The role of Cbl-b is unclear, however. Here, we show that overexpression of Cbl-b in T cells induced the constitutive activation of the transcription factor nuclear factor of activated T cells (NFAT). A loss-of-function mutation in Cbl-b disrupted the interaction between Cbl-b and Zap-70 and nearly completely abrogated the Cbl-b-mediated activation of NFAT. Unlike the proposed role of Cbl as a negative regulator, our results suggest that the Cbl homologue Cbl-b has a positive role in T-cell signaling, most likely via a direct interaction with the upstream kinase Zap-70." @default.
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• W2023561231 date "1999-02-01" @default.
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• W2023561231 title "A direct interaction between the adaptor protein Cbl-b and the kinase Zap-70 induces a positive signal in T cells" @default.
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• W2023561231 doi "https://doi.org/10.1016/s0960-9822(99)80090-6" @default.
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