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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells.

The molecular adapter c-Cbl is rapidly tyrosine phosphorylated following stimulation through the TCR and associates with Src homology domain-2 (SH2)/SH3 domain-containing adapters such as Grb2, Crk, and Crk-L, which interact with guanine nucleotide exchange factors specific for the Ras family. This suggests that c-Cbl may link TCR activation to molecules that regulate GTP binding proteins. The SH2/SH3-containing protein Vav also contains a guanine nucleotide exchange factor domain, and Vav has a crucial role in thymocyte development and activation of peripheral T cells following stimulation through the TCR. Here we show that Vav and c-Cbl form inducible molecular complexes in TCR-activated murine thymocytes and peripheral T cells as well as pervanadate-treated T cells. Vav/c-Cbl interactions are also detectable in freshly isolated T cells from gene- targeted mice that lack the T cell-specific inhibitory receptor CTLA-4, in which c-Cbl is hyperphosphorylated on tyrosine residues. The interaction between Vav and c-Cbl is directly mediated via the SH2 domain of Vav and is dependent on tyrosine phosphorylation of c-Cbl. In addition, we show that the conserved motif Y699 MTP present in c-Cbl is the binding site for the Vav SH2 domain in vitro. These data imply that c-Cbl is a molecular adapter that regulates the function of Vav in thymocytes and peripheral T cells.[1]


  1. Proto-oncoprotein Vav interacts with c-Cbl in activated thymocytes and peripheral T cells. Marengère, L.E., Mirtsos, C., Kozieradzki, I., Veillette, A., Mak, T.W., Penninger, J.M. J. Immunol. (1997) [Pubmed]
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