Biological role of arrestin-1 oligomerization

Srimal Samaranayake, Sergey A. Vishnivetskiy, Camilla R. Shores, Kimberly C. Thibeault, Seunghyi Kook, Jeannie Chen, Marie E. Burns, Eugenia V. Gurevich, Vsevolod V. Gurevich

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)8055-8069
Number of pages15
JournalJournal of Neuroscience
Issue number42
StatePublished - Oct 14 2020


  • Arrestin
  • Cell death
  • Oligomerization
  • Photoreceptor
  • Rod

ASJC Scopus subject areas

  • Neuroscience(all)


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