PT  - JOURNAL ARTICLE
AU  - Mohamed Aittaleb
AU  - Cassandra A Boguth
AU  - John J G Tesmer
TI  - STRUCTURE AND FUNCTION OF HETEROTRIMERIC G PROTEIN-REGULATED RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS
AID  - 10.1124/mol.109.061234
DP  - 2009 Oct 30
TA  - Molecular Pharmacology
PG  - mol.109.061234
4099  - http://molpharm.aspetjournals.org/content/early/2009/10/30/mol.109.061234.short
4100  - http://molpharm.aspetjournals.org/content/early/2009/10/30/mol.109.061234.full
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