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- W2079138949 abstract "The protooncogenic protein Vav has the structure of an intracellular signal transducer. It is exclusively expressed in cells of hematopoietic lineage and plays a crucial role in hematopoietic cell differentiation. Here we report that both in cell extracts and within intact mammalian cells Vav binds to Grb2 (Sem-5/ASH/Drk), an adaptor molecule which plays a key role in Ras activation. The interaction became evident from a yeast two-hybrid screen and its specificity was demonstrated by in vitro binding assays. It is mediated by an unusual protein-protein binding reaction: dimerization of specific intact Src homology 3 domains of each of the partners. Signaling during hematopoietic lineage differentiation may therefore involve the tissue-specific signal transducer Vav linking into the ubiquitous pathway involving Grb2 and ultimately Ras." @default.
- W2079138949 created "2016-06-24" @default.
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- W2079138949 date "1994-12-20" @default.
- W2079138949 modified "2023-09-26" @default.
- W2079138949 title "Binding of Vav to Grb2 through dimerization of Src homology 3 domains." @default.
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- W2079138949 doi "https://doi.org/10.1073/pnas.91.26.12629" @default.
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