Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Two-State Receptor Model01:29

The Two-State Receptor Model

3.6K
The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with...
3.6K
Antihypertensive Drugs: Action of Calcium Channel Blockers01:18

Antihypertensive Drugs: Action of Calcium Channel Blockers

2.3K
Calcium ions are essential to contract smooth muscle cells in blood vessels. They enter these cells through voltage-dependent calcium channels, specifically L-type calcium channels in the cell membrane. These L-type calcium channels are integral to the excitation-contraction coupling process in smooth muscle. When a stimulus is received by smooth muscle cells, their membrane depolarizes. This alteration in membrane potential instigates the opening of L-type calcium channels. As a result,...
2.3K
Relaxation of Skeletal Muscles01:29

Relaxation of Skeletal Muscles

10.5K
The period of muscle contraction primarily influences the duration of stimulation at the neuromuscular junction (NMJ), the presence of free calcium ions in the sarcoplasm, and the availability of energy or ATP to support contractions.
When an action potential reaches the axon terminal, it depolarizes the membrane and opens voltage-gated sodium channels. Sodium ions enter the cell, further depolarizing the presynaptic membrane. This depolarization causes voltage-gated calcium channels to open....
10.5K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

4.9K
Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
4.9K
Cross-bridge Cycle01:26

Cross-bridge Cycle

125.5K
As muscle contracts, the overlap between the thin and thick filaments increases, decreasing the length of the sarcomere—the contractile unit of the muscle—using energy in the form of ATP. At the molecular level, this is a cyclic, multistep process that involves binding and hydrolysis of ATP, and movement of actin by myosin.
125.5K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

8.1K
Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
8.1K

You might also read

Related Articles

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

Sort by
Same author

Dynamic regulation of PLCĪ¶ by Calmodulin and MARCKS may underlie Calcium oscillations during human fertilisation.

Cell calciumĀ·2026
Same author

The emerging role of calsequestrin 2: from calcium sensor and modulator to arrhythmia driver.

Journal of physiology and biochemistryĀ·2026
Same author

Compromised repolarization reserve in a murine model of catecholaminergic polymorphic ventricular tachycardia caused by RyR2-R420Q mutation.

Journal of molecular and cellular cardiologyĀ·2025
Same author

Disparate molecular mechanisms in cardiac ryanodine receptor channelopathies.

Frontiers in molecular biosciencesĀ·2025
Same author

Divergent Biochemical Properties and Disparate Impact of Arrhythmogenic Calmodulin Mutations on Zebrafish Cardiac Function.

Journal of cellular biochemistryĀ·2024
Same author

Development of Recombinant PLC-Zeta Protein as a Therapeutic Intervention for the Clinical Treatment of Oocyte Activation Failure.

BiomedicinesĀ·2024

Related Experiment Video

Updated: Apr 12, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

8.0K

Structural and functional interactions within ryanodine receptor.

Monika Seidel1, F Anthony Lai1, Spyros Zissimopoulos1

  • 1*Wales Heart Research Institute, Cardiff University School of Medicine, Institute of Molecular and Experimental Medicine, Heath Park, Cardiff CF14 4XN, U.K.

Biochemical Society Transactions
|May 27, 2015
PubMed
Summary

Ryanodine receptors are crucial for muscle function. This review explores how their subunit interactions impact muscle disorders and cardiac disease.

More Related Videos

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

12.2K
Functional Characterization of Endogenously Expressed Human RYR1 Variants
07:59

Functional Characterization of Endogenously Expressed Human RYR1 Variants

Published on: June 9, 2021

3.1K

Related Experiment Videos

Last Updated: Apr 12, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
11:31

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

8.0K
Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study
12:43

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

12.2K
Functional Characterization of Endogenously Expressed Human RYR1 Variants
07:59

Functional Characterization of Endogenously Expressed Human RYR1 Variants

Published on: June 9, 2021

3.1K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Physiology

Background:

  • The ryanodine receptor (RyR) is a critical Ca2+ release channel essential for muscle excitation-contraction coupling.
  • Dysregulation of RyR function is implicated in serious health conditions, including neuromuscular disorders and cardiac arrhythmias.

Purpose of the Study:

  • To review the structural mechanisms governing ryanodine receptor (RyR) channel regulation.
  • To elucidate the role of intra- and inter-subunit interactions in RyR function.
  • To connect these interactions to the pathophysiology of RyR-related diseases.

Main Methods:

  • Literature review of structural and functional studies on ryanodine receptors.
  • Analysis of research on intra- and inter-subunit interactions within the RyR complex.
  • Synthesis of findings linking RyR structural dynamics to disease mechanisms.

Main Results:

  • Intra- and inter-subunit interactions are key determinants of RyR channel gating and activity.
  • Specific structural alterations in these interactions can lead to channel dysfunction.
  • These dysfunctions directly contribute to the development of neuromuscular and cardiac pathologies.

Conclusions:

  • Understanding RyR subunit interactions provides critical insights into muscle and cardiac disease.
  • Targeting these interactions may offer novel therapeutic strategies for RyR-related disorders.
  • Further structural and functional studies are needed to fully unravel RyR regulation and its pathological consequences.