Document Detail


Identification of critical phosphorylation sites on the carboxy tail of melanopsin.
MedLine Citation:
PMID:  24678795     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Light activated opsins undergo carboxy terminal phosphorylation, which contributes to the deactivation of their photoresponse. The photopigment melanopsin possesses an unusually long carboxy tail containing 37 serine and threonine sites that are potential sites for phosphorylation by a G-protein dependent kinase (GRK). Here we show that a small cluster of 6-7 sites is sufficient for deactivation of light-activated mouse melanopsin. Surprisingly, these sites are distinct from those that regulate deactivation of rhodopsin. In zebrafish, there are 5 different melanopsin genes that encode proteins with distinct carboxy terminal domains. Naturally occurring changes in the same cluster of phosphorylatable amino acids provides diversity in the deactivation kinetics of the zebrafish proteins . These results suggest that variation in phosphorylation sites provides flexibility in the duration and kinetics of melanopsin-mediated light responses.
Authors:
Joseph R Blasic; Vanessa Matos-Cruz; Devyani Ujla; Evan Cameron; Samer Hattar; Marnie E Halpern; Phyllis R Robinson
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-3-31
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2014 Mar 
Date Detail:
Created Date:  2014-3-31     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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