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Updated: Apr 4, 2026

A Rhodopsin Transport Assay by High-Content Imaging Analysis

A Rhodopsin Transport Assay by High-Content Imaging Analysis

Published on: January 16, 2019

Misfolded opsin mutants display elevated β-sheet structure.

Lisa M Miller¹, Megan Gragg², Tae Gyun Kim³

¹National Synchrotron Light Source-II, Brookhaven National Laboratory, Upton, NY 11973, USA.

|September 12, 2015

Summary

This summary is machine-generated.

Misfolded opsin mutants, G188R and P23H, form aggregates in the endoplasmic reticulum, altering their structure and contributing to retinitis pigmentosa. This structural change, not ER retention, drives disease progression.

Keywords:

G protein-coupled receptor Membrane protein Protein aggregation Protein misfolding Retinal degeneration Secondary structure

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

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Published on: June 23, 2018

Area of Science:

Molecular biology
Cell biology
Biochemistry

Background:

Mutations in rhodopsin, a key visual receptor, can lead to misfolding and aggregation.
This aberrant protein processing is implicated in the pathogenesis of retinitis pigmentosa, a severe retinal degenerative disease.
The precise structural changes and cellular consequences of opsin misfolding remain incompletely understood.

Purpose of the Study:

To investigate the intracellular structures formed by specific opsin mutants (G188R and P23H) associated with autosomal dominant retinitis pigmentosa.
To elucidate the secondary structural alterations and aggregation patterns of these misfolded opsins within cells.
To determine if endoplasmic reticulum retention is the primary driver of cellular toxicity for these mutants.

Main Methods:

Utilized Förster resonance energy transfer (FRET) and Fourier transform infrared (FTIR) microspectroscopy.
Applied these techniques to probe intracellular structures of G188R and P23H opsin mutants within cells.
Analyzed changes in protein secondary structure (α-helical and β-sheet content) and aggregation.

Main Results:

Both G188R and P23H opsin mutants were found to form aggregates within the endoplasmic reticulum.
A significant alteration in secondary structure was observed, characterized by an increase in β-sheet content and a decrease in α-helical content.
The observed structural changes and aggregation were independent of the mere retention of opsin molecules in the endoplasmic reticulum.

Conclusions:

Misfolded opsin mutants adopt altered secondary structures, notably increased β-sheet content, which may promote their aggregation.
These structural changes and subsequent aggregation within the endoplasmic reticulum are key events in the pathogenesis of these forms of retinitis pigmentosa.
Cellular toxicity in these cases is linked to the structural consequences of misfolding rather than solely to the misfolded proteins being trapped in the ER.