Structure and Function of Heterotrimeric G Protein-Regulated Rho Guanine Nucleotide Exchange Factors
Autor: | Cassandra A. Boguth, Mohamed Aittaleb, John J.G. Tesmer |
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Rok vydání: | 2009 |
Předmět: |
Pharmacology
GTPase-activating protein G protein Minireviews macromolecular substances GTPase Biology Heterotrimeric GTP-Binding Proteins Receptors G-Protein-Coupled Cell biology G beta-gamma complex Biochemistry Heterotrimeric G protein G12/G13 alpha subunits Animals Guanine Nucleotide Exchange Factors Humans Molecular Medicine Rho Guanine Nucleotide Exchange Factors Signal Transduction G protein-coupled receptor G alpha subunit |
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 |
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