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Related Experiment Video

Updated: May 15, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Posttranslational modification and quality control.

Xuejun Wang¹, J Scott Pattison, Huabo Su

¹Division of Basic Biomedical Sciences, Sanford School of Medicine of the University of South Dakota, 414 East Clark St, Vermillion, SD 57069, USA. xuejun.wang@usd.edu

Circulation Research

|January 19, 2013

Summary

This summary is machine-generated.

Cellular protein quality control prevents misfolded protein toxicity. Recent advances reveal how posttranslational modifications regulate these crucial mechanisms, impacting cardiac health and disease.

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Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

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Last Updated: May 15, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Area of Science:

Cellular Biology
Molecular Biology
Cardiovascular Research

Background:

Protein quality control (PQC) is essential for cellular health, preventing the accumulation of toxic misfolded proteins.
PQC involves chaperones and protein degradation systems, including the ubiquitin-proteasome system and autophagy.
Defective PQC and protein aggregation are implicated in various diseases, particularly cardiac pathologies.

Purpose of the Study:

To review recent advances in understanding posttranslational modification (PTM)-mediated regulation of intracellular quality control (IQC).
To highlight the role of PTMs in modulating the efficiency of protein degradation and organelle clearance pathways.
To discuss the involvement of PTM-regulated IQC in the pathogenesis of cardiac dysfunction.

Main Methods:

Literature review focusing on PTMs affecting chaperones, the ubiquitin-proteasome system, and autophagy.
Analysis of studies investigating the impact of PTMs on protein aggregate clearance and organelle quality control.
Examination of experimental evidence linking aberrant PQC to cardiac disease models.

Main Results:

Posttranslational modifications significantly influence the activity and substrate specificity of PQC machinery.
PTMs can either enhance or impair the degradation of misfolded proteins and the removal of damaged organelles.
Dysregulation of PTMs in PQC components contributes to the development and progression of heart failure.

Conclusions:

Posttranslational modifications are critical regulators of intracellular quality control mechanisms.
Targeting PTMs offers potential therapeutic strategies for improving PQC in cardiac diseases.
Further research into PTM-mediated regulation of PQC is crucial for understanding and treating heart failure.