A Ras-GTPase-Activating Protein SH3-Domain-Binding Protein | Zendy

Fabienne Parker | Zendy; Florence Maurier | Zendy; Isabelle Delumeau | Zendy; Marc Duchesne | Zendy; Didier Faucher | Zendy; Laurent Debüssche | Zendy; Anita Dugue | Zendy; Fabien Schweighoffer | Zendy; Bruno Tocqué | Zendy

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A Ras-GTPase-Activating Protein SH3-Domain-Binding Protein

Author(s) -

Fabienne Parker,

Florence Maurier,

Isabelle Delumeau,

Marc Duchesne,

Didier Faucher,

Laurent Debüssche,

Anita Dugue,

Fabien Schweighoffer,

Bruno Tocqué

Publication year - 1996

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.16.6.2561

Subject(s) - biology , sh3 domain , gtpase activating protein , binding domain , gtpase , microbiology and biotechnology , ribonucleoprotein , binding site , biochemistry , rna , signal transduction , gene , g protein , proto oncogene tyrosine protein kinase src

We report the purification of a Ras-GTPase-activating protein (GAP)-binding protein, G3BP, a ubiquitously expressed cytosolic 68-kDa protein that coimmunoprecipitates with GAP. G3BP physically associates with the SH3 domain of GAP, which previously had been shown to be essential for Ras signaling. The G3BP cDNA revealed that G3BP is a novel 466-amino-acid protein that shares several features with heterogeneous nuclear RNA-binding proteins, including ribonucleoprotein (RNP) motifs RNP1 and RNP2, an RG-rich domain, and acidic sequences. Recombinant G3BP binds effectively to the GAP SH3 domain G3BP coimmunoprecipitates with GAP only when cells are in a proliferating state, suggesting a recruitment of a GAP-G3BP complex when Ras is in its activated conformation.

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