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Related Concept Videos

Phosphorylation01:02

Phosphorylation

53.0K
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...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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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...
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Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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....
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

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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.
Major types that are helpful drug targets include:
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Updated: Nov 27, 2025

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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Phosphorylation Modifications Regulating Cardiac Protein Quality Control Mechanisms.

Sumita Mishra1, Brittany L Dunkerly-Eyring2, Gizem Keceli1

  • 1Division of Cardiology, Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, MD, United States.

Frontiers in Physiology
|December 7, 2020
PubMed
Summary

Protein quality control (PQC) is crucial for heart health. Impaired PQC and protein aggregation contribute to cardiac disease, but understanding phosphorylation

Keywords:
autophagycardiac diseasechaperonesphosphorylationproteasomeubiquitin enzymes

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Area of Science:

  • Cardiovascular Biology
  • Molecular Cardiology
  • Cellular Proteostasis

Background:

  • Cardiac diseases, including heart failure, are associated with compromised protein quality control (PQC).
  • Impaired clearance of misfolded proteins leads to aggregate formation, reducing cardiomyocyte viability and cardiac function.
  • The cardiomyocyte PQC system, involving chaperones and degradation pathways (proteasome, lysosome), is vital for cellular health.

Purpose of the Study:

  • To review recent advances in understanding phosphorylation's role in regulating PQC.
  • To explore the impact of these regulatory mechanisms on cardiac pathology.
  • To identify therapeutic opportunities targeting phosphorylation in heart disease.

Main Methods:

  • Literature review of recent studies on protein phosphorylation and PQC.
  • Analysis of the interplay between phosphorylation and protein degradation pathways.
  • Synthesis of findings related to cardiac disease pathogenesis and therapeutic strategies.

Main Results:

  • Phosphorylation emerges as a key regulator of PQC, capable of both enhancing and inhibiting its machinery.
  • Dysregulation of phosphorylation significantly impacts cardiac pathology by affecting protein aggregate levels and cellular function.
  • Targeting specific phosphorylation events presents a promising avenue for novel therapeutic interventions.

Conclusions:

  • Phosphorylation plays a critical, multifaceted role in modulating PQC within cardiomyocytes.
  • Understanding these phosphorylation-driven PQC mechanisms is essential for developing effective treatments for cardiac diseases.
  • Harnessing phosphorylation modifications offers significant therapeutic potential for improving cardiac function and treating heart failure.