Binding of Vav to Grb2 through dimerization of Src homology 3 domains.

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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Cell Cycle Proteins, DNA Mutational Analysis, GRB2 Adaptor Protein, Humans, Mice, Molecular Sequence Data, Peptides, Protein Binding, Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-vav, Signal Transduction, Structure-Activity Relationship
Proc. Natl. Acad. Sci. U.S.A.
Date: Dec. 20, 1994
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