Functional Role of Arrestin-1 Residues Interacting with Unphosphorylated Rhodopsin Elements.

ABSTRACT: Arrestin-1, or visual arrestin, exhibits an exquisite selectivity for light-activated phosphorylated rhodopsin (P-Rh*) over its other functional forms. That selectivity is believed to be mediated by two well-established structural elements in the arrestin-1 molecule, the activation sensor detecting the active conformation of rhodopsin and the phosphorylation sensor responsive to the rhodopsin phosphorylation, which only active phosphorylated rhodopsin can engage simultaneously. However, in the crystal structure of the arrestin-1-rhodopsin complex there are arrestin-1 residues located close to rhodopsin, which do not belong to either sensor. Here we tested by site-directed mutagenesis the functional role of these residues in wild type arrestin-1 using a direct binding assay to P-Rh* and lig

SUBMITTER: Vishnivetskiy SA 

PROVIDER: S-EPMC10219436 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature