PUBLICATION

Identification of critical phosphorylation sites on the carboxy tail of melanopsin

Authors
Blasic, J.R., Matos-Cruz, V., Ujla, D., Cameron, E.G., Hattar, S., Halpern, M.E., Robinson, P.R.
ID
ZDB-PUB-140513-257
Date
2014
Source
Biochemistry   53: 2644-9 (Journal)
Registered Authors
Halpern, Marnie E., Matos-Cruz, Vanessa
Keywords
none
MeSH Terms
  • Amino Acid Sequence
  • Animals
  • HEK293 Cells
  • Humans
  • Kinetics
  • Light
  • Mice
  • Molecular Sequence Data
  • Multigene Family
  • Mutation
  • Phosphorylation
  • Protein Structure, Tertiary
  • Rod Opsins/genetics
  • Rod Opsins/metabolism*
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
PubMed
24678795 Full text @ Biochemistry
Abstract
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 regulate deactivation of rhodopsin. In zebrafish, there are five 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.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping