Journal
BIOCHEMICAL JOURNAL
Volume 375, Issue -, Pages 503-515Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20031076
Keywords
adapter protein; beta-arrestin; desensitization; endocytosis; G-protein-coupled receptor (GPCR); seven-membrane-spanning receptor (7MSR)
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Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL070631, R01HL016037, R37HL016037] Funding Source: NIH RePORTER
- NHLBI NIH HHS [HL70631, HL16037] Funding Source: Medline
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beta-Arrestins are cytosolic proteins that bind to activated and phosphorylated G-protein-coupled receptors [7MSRs (seven-membrane-spanning receptors)] and uncouple them from G-protein-mediated second messenger signalling pathways. The binding of beta-affestins to 7MSRs also leads to new signals via activation of MAPKs (mitogen-activated protein kinases) such as JNK3 (c-Jun N-terminal kinase 3), ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38 MAPKs. By binding to endocytic proteins [clathrin, AP2 (adapter protein 2), NSF (N-ethyl-maleimide-sensitive fusion protein) and ARF6 (ADP-ribosylation factor 6)], beta-arrestins also serve as adapters to link the receptors to the cellular trafficking machinery. Agonist-promoted ubiquitination of beta-arrestins is a prerequisite for their role in receptor internalization, as well as a determinant of the differing trafficking patterns of distinct classes of receptors. Recently, beta-arresfins have also been implicated as playing novel roles in cellular chemotaxis and apoptosis. By virtue of their ability to bind, in a stimulus-dependent fashion, to 7MSRs as well as to different classes of cellular proteins, beta-arrestins serve as versatile adapter proteins that regulate the signalling and trafficking of the receptors.
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