Structure and Function of Heterotrimeric G Protein-Regulated Rho Guanine Nucleotide Exchange Factors

Autor: Cassandra A. Boguth, Mohamed Aittaleb, John J.G. Tesmer
Rok vydání: 2009
Předmět:
Zdroj: Molecular Pharmacology. 77:111-125
ISSN: 1521-0111
0026-895X
DOI: 10.1124/mol.109.061234
Popis: 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 Galpha(12/13), Galpha(q), and Gbetagamma 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.
Databáze: OpenAIRE