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Related Concept Videos

Phosphorylation01:02

Phosphorylation

50.3K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
50.3K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

13.1K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
13.1K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.2K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
5.2K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.8K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.8K
Polarity of the Cytoskeleton01:18

Polarity of the Cytoskeleton

17.6K
The intrinsic polarity of cells can be primarily attributed to two factors- i) the asymmetric accumulation of mobile components such are regulatory molecules and subcellular components across the cell and ii) the orientation of polar cytoskeletal filaments that make up the cytoskeletal networks, specifically microfilaments, and microtubules arranged along the axis of polarity. Interactions between the cytoskeletal filaments are crucial for the establishment and maintenance of the polar nature...
17.6K
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

2.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K

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Related Experiment Video

Updated: Jul 1, 2025

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

11.7K

RyR2 phosphorylation alters dyad architecture.

Ben Short1

  • 1Science Writer, Rockefeller University Press , New York, NY, USA.

The Journal of General Physiology
|March 7, 2024
PubMed
Summary

Beta-adrenergic signaling enlarges dyads and reorganizes ryanodine receptor 2 (RyR2) tetramers in cardiomyocytes. This study reveals structural changes in cardiac cells due to this signaling pathway.

Area of Science:

  • Cardiology
  • Cell Biology
  • Physiology

Background:

  • Beta-adrenergic signaling is crucial for regulating cardiac function.
  • Understanding structural changes in cardiomyocytes is key to cardiac health.

Purpose of the Study:

  • To investigate the structural impact of beta-adrenergic signaling on cardiomyocyte dyads.
  • To examine the reorganization of ryanodine receptor 2 (RyR2) tetramers.

Main Methods:

  • Utilized advanced imaging techniques to visualize cardiomyocyte structures.
  • Analyzed the effects of beta-adrenergic stimulation on dyad morphology and RyR2 arrangement.

Main Results:

  • Beta-adrenergic signaling was found to enlarge dyads in cardiomyocytes.

More Related Videos

Oligopeptide Competition Assay for Phosphorylation Site Determination
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Oligopeptide Competition Assay for Phosphorylation Site Determination

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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

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Related Experiment Videos

Last Updated: Jul 1, 2025

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

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Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

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Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
08:55

Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag

Published on: December 14, 2017

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  • Significant reorganization of RyR2 tetramers was observed within these dyads.

    • Conclusions:

    • Beta-adrenergic signaling induces substantial structural remodeling of dyads and RyR2 complexes in cardiomyocytes.
    • These findings provide insights into the molecular mechanisms underlying cardiac adaptation to adrenergic stimuli.