A Ras-GTPase-Activating Protein SH3-Domain-Binding Protein
Open Access
- 1 June 1996
- journal article
- Published by Taylor & Francis in Molecular and Cellular Biology
- Vol. 16 (6) , 2561-2569
- https://doi.org/10.1128/mcb.16.6.2561
Abstract
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.Keywords
This publication has 72 references indexed in Scilit:
- The Human p62 cDNA Encodes Sam68 and Not the RasGAP-Associated p62 ProteinCell, 1996
- The role of p21ras in receptor tyrosine kinase signallingBiochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1994
- Activation of Phosphatidylinositol-3′ Kinase by Src-Family Kinase SH3 Binding to the p85 SubunitScience, 1994
- hnRNP PROTEINS AND THE BIOGENESIS OF mRNAAnnual Review of Biochemistry, 1993
- Identification of a Ten-Amino Acid Proline-Rich SH3 Binding SiteScience, 1993
- Identification of the SH3 Domain of GAP as an Essential Sequence for Ras-GAP-Mediated SignalingScience, 1993
- SH3 — an abundant protein domain in search of a functionFEBS Letters, 1992
- Molecular cloning of cDNAs encoding the GAP-associated protein p190: Implications for a signaling pathway from ras to the nucleusCell, 1992
- Gap Domains Responsible for Ras P21-Dependent Inhibition of Muscarinic Atrial K + Channel CurrentsScience, 1992
- Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferaseGene, 1988