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Abstract
<p class="first" id="d12347919e65">Upon their discovery, beta-arrestins 1 and 2 were
named for their capacity to sterically
hinder the G protein coupling of agonist-activated seven-transmembrane receptors,
ultimately resulting in receptor desensitization. Surprisingly, recent evidence shows
that beta-arrestins can also function to activate signaling cascades independently
of G protein activation. By serving as multiprotein scaffolds, the beta-arrestins
bring elements of specific signaling pathways into close proximity. beta-Arrestin
regulation has been demonstrated for an ever-increasing number of signaling molecules,
including the mitogen-activated protein kinases ERK, JNK, and p38 as well as Akt,
PI3 kinase, and RhoA. In addition, investigators are discovering new roles for beta-arrestins
in nuclear functions. Here, we review the signaling capacities of these versatile
adapter molecules and discuss the possible implications for cellular processes such
as chemotaxis and apoptosis.
</p>
[1
]Howard Hughes Medical Institute and Departments of 2Medicine and 3Biochemistry, Duke
University Medical Center, Durham, North Carolina 27710; email: