G protein-coupled receptor interacting proteins: emerging roles in localization and signal transduction.
The mechanism by which G protein-coupled receptors (GPCRs) translate extracellular signals into cellular changes initially was envisioned as a simple linear model: activation of the receptor by agonist binding leads to dissociation of the heterotrimeric GTP-binding G protein into its alpha and betagamma subunits, both of which can activate or inhibit various downstream effector molecules. The plethora of recently described multidomain scaffolding proteins and accessory/chaperone molecules that interact with GPCR, including GPCR themselves as homo- or heterodimers, provides for diverse molecular mechanisms for ligand recognition, signalling specificity, and receptor trafficking. This review will summarize the recently described GPCR-interacting proteins and their individual functional roles, as understood. Implicit in the search for the functional relevance of these interactions is the expectation that enhancement or disruption of target cell-specific events could serve as highly selective therapeutic opportunities.
Brady
Ashley E
AE
Vanderbilt University Medical Center, 464A Robinson Research Building, 37232-6600, Nashville, TN, USA
Limbird
Lee E
LE
D002462:Cell Membrane / Q000378:metabolism; D019281:Dimerization; D020962:Heterotrimeric GTP-Binding Proteins / Q000378:metabolism*; D046911:Macromolecular Substances; D018832:Molecular Chaperones / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000378:metabolism; D015398:Signal Transduction
D046911:Macromolecular Substances; D018832:Molecular Chaperones; D011956:Receptors, Cell Surface; D020962:Heterotrimeric GTP-Binding Proteins