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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...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...
Channel Rhodopsins01:11

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
GPCR Desensitization01:12

GPCR Desensitization

G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...

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Related Experiment Video

Updated: Jun 13, 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

Palmitoylation stabilizes unliganded rod opsin.

Akiko Maeda1, Kiichiro Okano, Paul S-H Park

  • 1Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106-4965, USA.

Proceedings of the National Academy of Sciences of the United States of America
|April 21, 2010
PubMed
Summary

Rhodopsin S-palmitoylation is crucial for retinal stability, preventing light-induced degeneration. Its absence causes rapid retinal damage, highlighting a structural role beyond signaling in G protein-coupled receptors (GPCRs).

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Published on: January 16, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Ophthalmology

Background:

  • S-palmitoylation is a common modification in G protein-coupled receptors (GPCRs), including rhodopsin.
  • The functional significance of rhodopsin S-palmitoylation on signaling has been considered modest.

Purpose of the Study:

  • To investigate the role of rhodopsin S-palmitoylation in vivo, particularly its impact on retinal integrity and light-induced responses.
  • To determine whether rhodopsin instability or aberrant signaling underlies pathology in palmitoylation-deficient models.

Main Methods:

  • Generation and analysis of palmitoylation-deficient (Palm(-/-)) mice with mutations in the opsin gene.
  • Cross-breeding Palm(-/-) mice with Lrat(-/-) mice (lacking retinoid binding) and Gnat1(-/-) mice (lacking G protein signaling).
  • Assessment of retinal degeneration, cellular deposits, and response to artificial chromophore treatment.

Main Results:

  • Palm(-/-) mice exhibited severe light-induced retinal degeneration affecting rod and cone cells.
  • Retinas showed nucleic acid deposits and infiltrating macrophages.
  • Crossing with Lrat(-/-) mice led to rapid degeneration in young animals, preventable by chromophore precursor treatment.
  • Eliminating G protein signaling in Palm(-/-)Gnat1(-/-) mice did not prevent degeneration.

Conclusions:

  • Rhodopsin S-palmitoylation plays a critical structural role in maintaining retinal stability and preventing light-induced degeneration.
  • The pathology observed is primarily due to the instability of unpalmitoylated opsin, not aberrant signal transduction.
  • These findings suggest a broader structural role for S-palmitoylation in GPCRs.