These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Modular architecture and novel protein-protein interactions regulating the RGS-containing Rho guanine nucleotide exchange factors.
    Author: Vázquez-Prado J, Basile J, Gutkind JS.
    Journal: Methods Enzymol; 2004; 390():259-85. PubMed ID: 15488183.
    Abstract:
    The regulator of G-protein signaling (RGS)-containing RhoGEFs, including p115RhoGEF, PDZ-RhoGEF, and LARG, represent a novel family of guanine nucleotide exchange factors for RhoA that are regulated by the Galpha(12/13) family of heterotrimeric G proteins. Experimental evidence indicates that the complex architecture of these RhoGEFs provides the structural basis for novel regulatory mechanisms mediated by protein-protein interactions. These include the direct association of their RGS domain with GTP-bound forms of Galpha(12/13) and the binding of the PDZ domain present in PDZ-RhoGEF and LARG to plexins, which are receptors for semaphorins. The carboxyl-terminal region of these GEFs also exerts regulatory properties, including the ability to form dimers, which is inhibitory to their in vivo GEF activity and, in the case of PDZ-RhoGEF, to associate with PAK4, a downstream target of Cdc42. This carboxyl-terminal region also acts as the target for tyrosine kinases, which have a positive effect on the long-term activity of these GEFs. This article describes the experimental strategies that have been utilized to begin unraveling the molecular mechanisms regulating the functional activity of RGS-containing RhoGEFs.
    [Abstract] [Full Text] [Related] [New Search]