# Structure-function studies of visual arrestin

> **NIH NIH R01** · VANDERBILT UNIVERSITY · 2024 · $542,070

## Abstract

Project Summary
We propose to elucidate fine molecular mechanism of arrestin-1 interaction with rhodopsin, focusing on
the aspects of this mechanism that ensure remarkable selectivity of arrestin-1 for light-activated
phosphorylated rhodopsin and much lower binding to all other functional forms of rhodopsin (inactive
phosphorylated, light-activated unphosphorylated, inactive unphosphorylated, opsin, and phosphorylated
opsin). We propose to design “enhanced” arrestin-1 mutants with high binding to unphosphorylated light-
activated rhodopsin. We expect these mutants to compensate for defects in rhodopsin phosphorylation in
vivo. Mutants of this kind have therapeutic potential in human visual disorders caused by absent or
insufficient rhodopsin phosphorylation. Based on the discoveries of non-rhodopsin binding partners of
arrestin-1 we propose to use in vivo proximity labeling to identify novel arrestin-1 interaction partners in
rod photoreceptors. These partners will be biotinylated by AirID fused to arrestin-1 (we validated both
functions of the two fusions we propose to use), purified via biotin binding to avidin, digested into
peptides, which will be identified by mass spectrometry (LC-MS/MS).

## Key facts

- **NIH application ID:** 10981996
- **Project number:** 2R01EY011500-27
- **Recipient organization:** VANDERBILT UNIVERSITY
- **Principal Investigator:** VSEVOLOD V. GUREVICH
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $542,070
- **Award type:** 2
- **Project period:** 1997-04-01 → 2028-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10981996

## Citation

> US National Institutes of Health, RePORTER application 10981996, Structure-function studies of visual arrestin (2R01EY011500-27). Retrieved via AI Analytics 2026-05-24 from https://api.ai-analytics.org/grant/nih/10981996. Licensed CC0.

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