RhoA co-ordinates with heterotrimeric G proteins to regulate efficacy.
Heterotrimeric G proteins have a critical role in mediating signal transduction by ligand-stimulated GPCRs. While activation of heterotrimeric G proteins is known to proceed via the G protein guanine nucleotide cycle, there is much uncertainty regarding the process that determines efficacy, the extent of response across signaling pathways. Gα(GTP) can interact with multiple binding partners, including several effectors and regulators. Cross-talk by other receptor-signaling pathways can alter the response. It remains unclear whether G protein efficacy is regulated. This lack of clarity impairs our ability to predict and manipulate the pharmacological behavior of activated G proteins. This review will discuss emerging evidence that implicates monomeric RhoA in the process that regulates G(q) efficacy.
Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL 33101-6189, USA. ilitosch@med.miami.edu
Irene
I
Litosch
D044385:GTP-Binding Protein alpha Subunits / Q000378:metabolism*; D010712:Phosphatidic Acids / Q000096:biosynthesis / Q000378:metabolism*; D043562:Receptors, G-Protein-Coupled / Q000378:metabolism*; D020742:rhoA GTP-Binding Protein / Q000378:metabolism*
D044385:GTP-Binding Protein alpha Subunits; D010712:Phosphatidic Acids; D043562:Receptors, G-Protein-Coupled; D020742:rhoA GTP-Binding Protein