Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 43, Issue 6, Pages 412-423Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2018.03.005
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Funding
- NIH [R35 GM122491, EY011500, DA043680, GM095633, GM120569]
- NATIONAL EYE INSTITUTE [R01EY011500] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM109955, R01GM077561, R01GM095633, R01GM120569, R35GM122491, R01GM063097] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE ON DRUG ABUSE [R21DA043680] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [S10OD021483] Funding Source: NIH RePORTER
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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 effectorbinding sites.
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