Arrestins: ubiquitous regulators of cellular signaling pathways |
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Authors: | Eugenia V Gurevich Vsevolod V Gurevich |
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Institution: | (1) Department of Pharmacology, Vanderbilt University, 2200 Pierce Avenue, Preston Research Building, Nashville, TN 37232, USA; |
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Abstract: | In vertebrates, the arrestins are a family of four proteins that regulate the signaling and trafficking of hundreds of different
G-protein-coupled receptors (GPCRs). Arrestin homologs are also found in insects, protochordates and nematodes. Fungi and
protists have related proteins but do not have true arrestins. Structural information is available only for free (unbound)
vertebrate arrestins, and shows that the conserved overall fold is elongated and composed of two domains, with the core of
each domain consisting of a seven-stranded β-sandwich. Two main intramolecular interactions keep the two domains in the correct
relative orientation, but both of these interactions are destabilized in the process of receptor binding, suggesting that
the conformation of bound arrestin is quite different. As well as binding to hundreds of GPCR subtypes, arrestins interact
with other classes of membrane receptors and more than 20 surprisingly diverse types of soluble signaling protein. Arrestins
thus serve as ubiquitous signaling regulators in the cytoplasm and nucleus. |
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