Search research articles

Search research articles

Related Experiment Videos

Evidence for conformational coupling between two calcium channels.

C Paolini¹, James D Fessenden, Isaac N Pessah

¹Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, PA 19104-6058, USA.

Proceedings of the National Academy of Sciences of the United States of America

|August 18, 2004

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Proposed key characteristics of neurotoxic chemicals.

Neurotoxicology·2025

Same author

Structure-activity of Bastadins from the marine sponge Ianthella basta. Modulators of the RYR1 Ca<sup>2+</sup> channel.

Bioorganic & medicinal chemistry letters·2025

Same author

The α4 Nicotinic Acetylcholine Receptor Is Necessary for the Initiation of Organophosphate-Induced Neuronal Hyperexcitability.

Toxics·2024

Same author

The Piezo channel is a mechano-sensitive complex component in the mammalian inner ear hair cell.

Nature communications·2024

Same author

<i>Ex vivo</i> exposure to polybrominated diphenyl ether (PBDE) selectively affects the immune response in autistic children.

Brain, behavior, & immunity - health·2023

Same author

The Piezo channel is central to the mechano-sensitive channel complex in the mammalian inner ear.

Research square·2023

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Ryanodine treatment shifts alpha(1S)dihydropyridine receptor positions, revealing structural changes in the ryanodine receptor 1 complex. This indicates the alpha(1S)dihydropyridine receptor-ryanodine receptor complex functions as a single unit.

Area of Science:

Muscle physiology
Molecular biology
Biophysics

Background:

Ryanodine receptor 1 (RyR1) and alpha(1S)dihydropyridine receptor (DHPR) are crucial for skeletal muscle excitation-contraction coupling.
These receptors, located in separate membrane systems, are known to be functionally and structurally linked.
A tetrad of DHPRs is associated with each RyR, forming a functional complex.

Purpose of the Study:

To investigate the structural integrity of the DHPR-RyR1 complex.
To determine if ryanodine, a RyR1 blocker, induces conformational changes in the complex.
To assess the functional relationship between RyR1 and DHPR.

Main Methods:

Skeletal muscle cell lines were treated with ryanodine.
Ryanodine concentrations were used to block RyR1 activity.

Related Experiment Videos

Changes in the distance between DHPRs within the tetrad were measured.

Main Results:

Ryanodine treatment caused a significant shift (approximately 2 nm) in the positions of alpha(1S)DHPRs.
This positional shift indicates substantial conformational alterations within the RyR1 cytoplasmic domain.
The DHPR-RyR1 complex demonstrated coordinated structural responses.

Conclusions:

Ryanodine binding induces significant conformational changes in RyR1.
The alpha(1S)DHPR-RyR1 complex operates as an integrated functional unit.
These findings provide insights into the molecular mechanisms of skeletal muscle excitation-contraction.