Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13.

Science (New York, N.Y.) | Jun 26, 1998

Signaling pathways that link extracellular factors to activation of the monomeric guanosine triphosphatase (GTPase) Rho control cytoskeletal rearrangements and cell growth. Heterotrimeric guanine nucleotide-binding proteins (G proteins) participate in several of these pathways, although their mechanisms are unclear. The GTPase activities of two G protein alpha subunits, Galpha12 and Galpha13, are stimulated by the Rho guanine nucleotide exchange factor p115 RhoGEF. Activated Galpha13 bound tightly to p115 RhoGEF and stimulated its capacity to catalyze nucleotide exchange on Rho. In contrast, activated Galpha12 inhibited stimulation by Galpha13. Thus, p115 RhoGEF can directly link heterotrimeric G protein alpha subunits to regulation of Rho.

Pubmed ID: 9641916 RIS Download

Mesh terms: Aluminum Compounds | Animals | COS Cells | Fluorides | GTP Phosphohydrolases | GTP-Binding Protein alpha Subunits, G12-G13 | GTP-Binding Proteins | Guanine Nucleotide Exchange Factors | Guanosine 5'-O-(3-Thiotriphosphate) | Guanosine Diphosphate | Guanosine Triphosphate | Proteins | Recombinant Fusion Proteins | Recombinant Proteins | Signal Transduction

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.