The Grb2 adaptor
- 1 August 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 369 (1), 47-51
- https://doi.org/10.1016/0014-5793(95)00578-w
Abstract
Grb2 is an ‘adaptor’ protein made of one SH2 and two SH3 domains. The SH3 domains bind to prolinerich motifs in the C-terminal part of the ras exchange factor Sos. Binding of the Grb2 SH2 domain to phosphotyrosine motifs on receptors, or other adaptor proteins such as Shc, recruits this Grb2/Sos complex at the plasma membrane where Sos stimulates nucleotide exchange on ras, then ras activates raf and leads to MAP kinase activation. The structure of Grb2, the precise motifs recognised by its SH2 and SH3 domains, the way Grb2 performs its function, a possible regulation of its association with Sos, and its ability to complex with other proteins in vivo, are discussed.Keywords
This publication has 57 references indexed in Scilit:
- Crystal Structure of the Mammalian Grb2 AdaptorScience, 1995
- The regulation and function of p21ras during T-cell activation and growthImmunology Today, 1995
- Backwards and forwards bindingNature Structural & Molecular Biology, 1994
- The GRB2/Sem‐5 adaptor proteinFEBS Letters, 1994
- The Function of GRB2 in Linking the Insulin Receptor to Ras Signaling PathwaysScience, 1993
- Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 1993
- SH2 domains recognize specific phosphopeptide sequencesCell, 1993
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993