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The Grb2 adaptor
Author(s) -
Chardin Pierre,
Cussac Didier,
Maignan Sébastien,
Ducruix Arnaud
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00578-w
Subject(s) - grb2 , signal transducing adaptor protein , sh2 domain , sh3 domain , guanine nucleotide exchange factor , microbiology and biotechnology , biology , proto oncogene tyrosine protein kinase src , chemistry , signal transduction
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.