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Related Concept Videos

Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category, whereas...
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Related Experiment Video

Updated: May 19, 2026

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein
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Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein

Published on: October 4, 2024

BiP prevents rod opsin aggregation.

Dimitra Athanasiou1, Maria Kosmaoglou, Naheed Kanuga

  • 1UCL Institute of Ophthalmology, London, United Kingdom.

Molecular Biology of the Cell
|August 3, 2012
PubMed
Summary
This summary is machine-generated.

Binding immunoglobulin protein (BiP) prevents rod opsin aggregation, crucial for preventing retinitis pigmentosa. Inhibiting BiP causes rod opsin to aggregate in the endoplasmic reticulum, highlighting BiP's role in maintaining protein solubility.

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Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
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Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis

Published on: December 7, 2021

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Last Updated: May 19, 2026

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein
08:18

Methodology for Studying Interactions of Vitamin A Membrane Receptors and Opsin Protein with their Ligands in Generating the Retinylidene Protein

Published on: October 4, 2024

A Rhodopsin Transport Assay by High-Content Imaging Analysis
12:11

A Rhodopsin Transport Assay by High-Content Imaging Analysis

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Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
11:08

Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis

Published on: December 7, 2021

Area of Science:

  • Molecular biology
  • Cell biology
  • Genetics

Background:

  • Mutations in rod opsin, a key protein in rod photoreceptor cells, are a primary cause of retinitis pigmentosa.
  • Many of these mutations result in protein misfolding, underscoring the importance of molecular chaperones in proper protein biogenesis.

Purpose of the Study:

  • To investigate the role of the molecular chaperone Binding immunoglobulin protein (BiP, also known as HSPA5) in the biogenesis and solubility of rod opsin.
  • To determine the consequences of inhibiting BiP activity on wild-type and mutant rod opsin.

Main Methods:

  • Utilized fluorescence recovery after photobleaching to assess the mobility of wild-type (WT) and mutant (P23H) rod opsin fused to green fluorescent protein (GFP) in the endoplasmic reticulum (ER).
  • Employed the subtilase cytotoxin SubAB to cleave and inhibit BiP activity.
  • Investigated the effects of BiP inhibition and overexpression on rod opsin aggregation and ubiquitylation within the ER.

Main Results:

  • BiP was found to prevent the aggregation of rod opsin.
  • Inhibition of BiP activity using SubAB or a BiP mutant (BiP(T37G)) led to ER retention and ubiquitylation of WT rod opsin, significantly decreasing its mobility.
  • BiP overexpression enhanced the mobility of the misfolding P23H mutant rod opsin, indicating a role in reducing mutant protein aggregation.

Conclusions:

  • BiP is essential for maintaining the solubility of rod opsin within the endoplasmic reticulum.
  • Disruption of BiP function results in rod opsin aggregation, contributing to the cellular pathology associated with retinitis pigmentosa.