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- Title
Biological Role of Arrestin-1 Oligomerization.
- Authors
Samaranayake, Srimal; Vishnivetskiy, Sergey A.; Shores, Camilla R.; Thibeault, Kimberly C.; Kook, Seunghyi; Chen, Jeannie; Burns, Marie E.; Gurevich, Eugenia V.; Gurevich, Vsevolod V.
- Abstract
Members of the arrestin superfamily have great propensity of self-association, but the physiological significance of this phenomenon is unclear. To determine the biological role of visual arrestin-1 oligomerization in rod photoreceptors, we expressed mutant arrestin-1 with severely impaired self-association in mouse rods and analyzed mice of both sexes. We show that the oligomerization-deficient mutant is capable of quenching rhodopsin signaling normally, as judged by electroretinography and single-cell recording. Like wild type, mutant arrestin-1 is largely excluded from the outer segments in the dark, proving that the normal intracellular localization is not due the size exclusion of arrestin-1 oligomers. In contrast to wild type, supraphysiological expression of the mutant causes shortening of the outer segments and photoreceptor death. Thus, oligomerization reduces the cytotoxicity of arrestin-1 monomer, ensuring long-term photoreceptor survival.
- Subjects
OLIGOMERIZATION; PHOTORECEPTORS; OLIGOMERS; MONOMERS; ARRESTINS
- Publication
Journal of Neuroscience, 2020, Vol 40, Issue 42, p8055
- ISSN
0270-6474
- Publication type
Article
- DOI
10.1523/jneurosci.0749-20.2020