Ontology highlight
ABSTRACT:
SUBMITTER: Blasic JR
PROVIDER: S-EPMC4010260 | biostudies-literature | 2014 Apr
REPOSITORIES: biostudies-literature
Blasic Joseph R JR Matos-Cruz Vanessa V Ujla Devyani D Cameron Evan G EG Hattar Samer S Halpern Marnie E ME Robinson Phyllis R PR
Biochemistry 20140416 16
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 six to seven sites is sufficient for deactivation of light-activated mouse melanopsin. Surprisingly, these sites are distinct from those that ...[more]