RT Journal Article
SR Electronic
T1 STRUCTURE AND FUNCTION OF HETEROTRIMERIC G PROTEIN-REGULATED RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP mol.109.061234
DO 10.1124/mol.109.061234
A1 Mohamed Aittaleb
A1 Cassandra A Boguth
A1 John J G Tesmer
YR 2009
UL http://molpharm.aspetjournals.org/content/early/2009/10/30/mol.109.061234.abstract
AB Activation of certain classes of G protein-coupled receptors (GPCRs) can lead to alterations in the actin cytoskeleton, gene transcription, cell transformation, and other processes that are known to be regulated by Rho family small molecular weight GTPases. Although these responses can occur indirectly via cross-talk from canonical heterotrimeric G protein cascades, it has recently been demonstrated that Dbl family Rho guanine nucleotide exchange factors (RhoGEFs) can serve as the direct downstream effectors of heterotrimeric G proteins. Heterotrimeric Gα12/13, Gαq, and Gβγ subunits are each now known to directly bind and regulate RhoGEFs. Atomic structures have recently been determined for several of these RhoGEFs and their G protein complexes, providing fresh insight into the molecular mechanisms of signal transduction between GPCRs and small molecular weight G proteins. This review covers what is currently known about the structure, function, and regulation of these recently recognized effectors of heterotrimeric G proteins.The American Society for Pharmacology and Experimental Therapeutics