Structural Basis of Arrestin-Dependent Signal Transduction.

Chen Q, Iverson TM, Gurevich VV
Trends Biochem Sci. 2018 43 (6): 412-423

PMID: 29636212 · PMCID: PMC5959776 · DOI:10.1016/j.tibs.2018.03.005

Arrestins are a small family of proteins with four isoforms in humans. Remarkably, two arrestins regulate signaling from >800 G protein-coupled receptors (GPCRs) or nonreceptor activators by simultaneously binding an activator and one out of hundreds of other signaling proteins. When arrestins are bound to GPCRs or other activators, the affinity for these signaling partners changes. Thus, it is proposed that an activator alters arrestin's ability to transduce a signal. The comparison of all available arrestin structures identifies several common conformational rearrangements associated with activation. In particular, it identifies elements that are directly involved in binding to GPCRs or other activators, elements that likely engage distinct downstream effectors, and elements that likely link the activator-binding sites with the effector-binding sites.

Copyright © 2018 Elsevier Ltd. All rights reserved.

MeSH Terms (5)

Animals Arrestin Humans Models, Molecular Signal Transduction

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