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Related Concept Videos

Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
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,...
Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...

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Related Experiment Video

Updated: May 30, 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

Ryanodine receptors.

E Michelle Capes1, Randall Loaiza, Héctor H Valdivia

  • 1Department of Cellular and Regenerative Biology, University of Wisconsin Medical School, Madison, WI 53711, USA. hvaldivia@wisc.edu.

Skeletal Muscle
|July 30, 2011
PubMed
Summary

Ryanodine receptors (RyRs) control calcium release crucial for muscle contraction. Their precise regulation is vital, as dysfunction causes severe cardiac and skeletal muscle diseases.

Area of Science:

  • Muscle Physiology
  • Molecular Biology
  • Cardiovascular Research

Background:

  • Excitation-contraction coupling in striated muscle relies on calcium signaling.
  • Ryanodine receptors (RyRs) gate intracellular calcium release from the sarcoplasmic reticulum.
  • Proper RyR function is essential for muscle contraction and relaxation.

Purpose of the Study:

  • To review the structural and functional attributes of RyRs.
  • To elucidate the regulatory mechanisms governing RyR activity.
  • To discuss RyR dysfunction in cardiovascular diseases and skeletal myopathies.

Main Methods:

  • Review of existing literature on RyR structure, function, and regulation.
  • Analysis of pathogenic RyR mutations and their clinical implications.

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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
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Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

Published on: June 9, 2017

Related Experiment Videos

Last Updated: May 30, 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

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
10:13

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding

Published on: June 9, 2017

  • Integration of data on RyR's role as a signaling hub.

    • Main Results:

    • RyRs are critical regulators of intracellular calcium, integrating multiple signaling pathways.
    • RyR activity is modulated by cytosolic metabolites, luminal proteins, and post-translational modifications.
    • Dysregulation of RyR calcium release is linked to significant muscle pathologies.

    Conclusions:

    • RyRs are central to muscle function, acting as sophisticated molecular switchboards.
    • Understanding RyR regulation is key to addressing diseases associated with calcium handling.
    • Pathogenic RyR dysfunction underscores their importance in cardiac and skeletal health.