PUBLICATION

Interaction of G protein-coupled receptor kinases and recoverin isoforms is determined by localization in zebrafish photoreceptors

Authors
Ahrens, N., Elbers, D., Greb, H., Janssen-Bienhold, U., Koch, K.W.
ID
ZDB-PUB-210103-3
Date
2020
Source
Biochimica et biophysica acta. Molecular cell research   1868(4): 118946 (Journal)
Registered Authors
Keywords
G-protein-coupled receptor kinases, photoreceptor, protein-protein interaction, recoverin, zebrafish
MeSH Terms
  • Animals
  • Cloning, Molecular
  • G-Protein-Coupled Receptor Kinases/genetics
  • G-Protein-Coupled Receptor Kinases/metabolism*
  • Gene Expression Regulation
  • Photoreceptor Cells, Vertebrate/metabolism*
  • Protein Interaction Maps
  • Recoverin/genetics
  • Recoverin/metabolism*
  • Surface Plasmon Resonance
  • Zebrafish/metabolism*
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism
PubMed
33385424 Full text @ BBA Molecular Cell Research
Abstract
The zebrafish retina expresses four recoverin genes (rcv1a, rcv1b, rcv2a and rcv2b) and four opsin kinase genes (grk1a, grk1b, grk7a and grk7b) coding for recoverin and G protein-coupled receptor kinase (opsin kinase) paralogs, respectively. Both protein groups are suggested to form regulatory complexes in rod and cone outer segments, but at present, we lack information about co-localization of recoverin and opsin kinases in zebrafish retinae and which protein-protein interacting pairs form. We analyzed the distribution and co-localization of recoverin and opsin kinase expression in the zebrafish retina. For this purpose, we used custom-tailored monospecific antibodies revealing that the amount of recoverin paralogs in a zebrafish retina can differ by more than one order of magnitude with the highest amount for recoverin 1a and 2b. Further, immunohistochemical labelling showed presence of recoverin 1a in all rod cell compartments, but it only co-localized with opsin kinase 1a in rod outer segments. In contrast, recoverin 2b was only detected in double cones and co-localized with opsin kinases 1b, 7a and 7b. Further, we investigated the interaction between recoverin and opsin kinase variants by surface plasmon resonance spectroscopy indicating interaction of recoverin 1a and recoverin 2b with all opsin kinases. However, binding kinetics for recoverin 1a differed from those observed with recoverin 2b that showed slower association and dissociation processes. Our results indicate diverse recoverin and opsin kinase properties due to differential expression and interaction profiles.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping