title: β-Arrestins: modulators of small GTPase activation and function.
abstract: Most cellular events responsible for accurate G protein-coupled receptor trafficking involve small GTP-binding proteins. For example, trafficking of receptors via the endocytic and exocytic pathways requires activation of ADP-ribosylation factors and Rab proteins, while receptor-mediated complex responses such as migration are well characterized to be dependent upon Rho family members. Because β-arrestin proteins are recruited to activated receptors and now considered as key signaling molecules, whether they act to control small GTPase activity remains a subject of great interest. Over the years, considerable evidence has suggested that β-arrestins and GTPases might be effectors of the same signaling pathways. One example is the roles of both β-arrestin and Ras, the prototypical GTPase, in coordinating activation of mitogen-activated protein kinase. Recently developed tools effective in suppressing the expression of β-arrestins will help define whether they are essential for small G protein activation. Furthermore, novel approaches to identify protein complexes will greatly advance our understanding of the possible cross talk between β-arrestin and small GTPases.
authors.affiliation: Department of Pharmacology, Université de Montréal, Montréal, Quebec, Canada.
authors.forename: Audrey
authors.initials: A
authors.lastname: Claing
mesh_terms: D000818:Animals; D019390:Arrestins / Q000378:metabolism*; D004705:Endocytosis; D004789:Enzyme Activation; D006801:Humans; D008954:Models, Biological; D020559:Monomeric GTP-Binding Proteins / Q000378:metabolism*; D015398:Signal Transduction; D000071557:beta-Arrestins
chemical_list: D019390:Arrestins; D000071557:beta-Arrestins; D020559:Monomeric GTP-Binding Proteins