Binding of Vav to Grb2 through dimerization of Src homology 3 domains - PubMed (original) (raw)

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

Z S Ye et al. Proc Natl Acad Sci U S A. 1994.

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.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Cell. 1992 Aug 7;70(3):431-42 - PubMed
    1. Proc Natl Acad Sci U S A. 1991 Jan 15;88(2):627-31 - PubMed
    1. Nature. 1989 Jul 20;340(6230):245-6 - PubMed
    1. Cell Growth Differ. 1991 Feb;2(2):95-105 - PubMed
    1. Science. 1993 May 7;260(5109):822-5 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources