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.
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