Document Detail

The physiological roles of arrestin-1 in rod photoreceptor cells.
MedLine Citation:
PMID:  24292825     Owner:  NLM     Status:  In-Data-Review    
Arrestin-1 is the second most abundant protein in rod photoreceptors and is nearly equimolar to rhodopsin. Its well-recognized role is to "arrest" signaling from light-activated, phosphorylated rhodopsin, a prototypical G protein-coupled receptor. In doing so, arrestin-1 plays a key role in the rapid recovery of the light response. Arrestin-1 exists in a basal conformation that is stabilized by two independent sets of intramolecular interactions. The intramolecular constraints are disrupted by encountering (1) active conformation of the receptor (R*) and (2) receptor-attached phosphates. Requirement for these two events ensures its highly specific high-affinity binding to phosphorylated, light-activated rhodopsin (P-R*). In the dark-adapted state, the basal form is further organized into dimers and tetramers. Emerging data suggest pleiotropic roles of arrestin-1 beyond the functional range of rod cells. These include light-induced arrestin-1 translocation from the inner segment to the outer segment, a process that may be protective against cellular damage incurred by constitutive signaling. Its expanding list of binding partners also hints at additional, yet to be characterized functions. Uncovering these novel roles of arrestin-1 is a subject of future studies.
Jeannie Chen
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Handbook of experimental pharmacology     Volume:  219     ISSN:  0171-2004     ISO Abbreviation:  Handb Exp Pharmacol     Publication Date:  2014  
Date Detail:
Created Date:  2013-12-02     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7902231     Medline TA:  Handb Exp Pharmacol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  85-99     Citation Subset:  IM    
Department of Cell and Neurobiology, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA, USA,
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