This title appears in the Scientific Report :
2020
Please use the identifier:
http://hdl.handle.net/2128/25551 in citations.
Please use the identifier: http://dx.doi.org/10.1038/s41598-020-67944-0 in citations.
Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin
Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin
Termination of the G-protein-coupled receptor signaling involves phosphorylation of its C-terminus and subsequent binding of the regulatory protein arrestin. In the visual system, arrestin-1 preferentially binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. Here,...
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Personal Name(s): | Stadler, Andreas M. |
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Granzin, Joachim / Cousin, Anneliese / Batra-Safferling, Renu (Corresponding author) | |
Contributing Institute: |
Strukturbiochemie; IBI-7 Neutronenstreuung und biologische Materie; IBI-8 Neutronenstreuung; JCNS-1 Neutronenstreuung; ICS-1 |
Published in: | Scientific reports, 10 (2020) 1, S. 10938 |
Imprint: |
[London]
Macmillan Publishers Limited, part of Springer Nature
2020
|
DOI: |
10.1038/s41598-020-67944-0 |
PubMed ID: |
32616825 |
Document Type: |
Journal Article |
Research Program: |
Engineering Cell Function |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1038/s41598-020-67944-0 in citations.
Termination of the G-protein-coupled receptor signaling involves phosphorylation of its C-terminus and subsequent binding of the regulatory protein arrestin. In the visual system, arrestin-1 preferentially binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. Here, we have investigated binding of a synthetic phosphopeptide of bovine rhodopsin (residues 323–348) to the active variants of visual arrestin-1: splice variant p44, and the mutant R175E. Unlike the wild type arrestin-1, both these arrestins are monomeric in solution. Solution structure analysis using small angle X-ray scattering supported by size exclusion chromatography results reveal dimerization in both the arrestins in the presence of phosphopeptide. Our results are the first report, to our knowledge, on receptor-induced oligomerization in arrestin, suggesting possible roles for the cellular function of arrestin oligomers. Given high structural homology and the similarities in their activation mechanism, these results are expected to have implications for all arrestin isoforms. |