Mechanisms of amphibian arrestin 1 self-association and dynamic distribution in retinal photoreceptors.

ABSTRACT: Visual arrestin 1 (Arr1) is an essential protein for termination of the light response in photoreceptors. While mammalian Arr1s form dimers and tetramers at physiological concentrations in vitro, oligomerization in other vertebrates has not been studied. Here we examine self-association of Arr1 from two amphibian species, Xenopus laevis (xArr1) and Ambystoma tigrinum (salArr1). Sedimentation velocity analytical ultracentrifugation showed that xArr1 and salArr1 oligomerization is limited to dimers. The K_D for dimer formation was 53 μM for xArr1 and 44 μM for salArr1, similar to the 69 μM K_D for bovine Arr1 (bArr1) dimers. Mutations of orthologous amino acids important for mammalian Arr1 oligomerization had no impact on xArr1 dimerization. Crystallography showed that th

SUBMITTER: Barnes CL 

PROVIDER: S-EPMC11652889 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature