Journal Article

FZJ-2020-02297

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Phosphorylated peptide of G protein-coupled receptor induces dimerization in activated arrestin

Stadler, A. M.FZJ* ; Granzin, J.FZJ* ; Cousin, A.FZJ* ; Batra-Safferling, R. (Corresponding author)FZJ*

2020
Macmillan Publishers Limited, part of Springer Nature [London]

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Please use a persistent id in citations: http://hdl.handle.net/2128/25551  doi:10.1038/s41598-020-67944-0

Abstract: 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.

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Contributing Institute(s):

1. Strukturbiochemie (IBI-7)
2. Neutronenstreuung (ICS-1)
3. Neutronenstreuung (JCNS-1)
4. Neutronenstreuung und biologische Materie (IBI-8)

Research Program(s):

1. 552 - Engineering Cell Function (POF3-552) (POF3-552)

Appears in the scientific report 2020

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