Research Topic

Post-Translational Modifications and Compartmentalized Protein Quality Control in Cardiac Muscle and Disease

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About this Research Topic

Post-translational modifications (PTMs) increase the functional diversity of the proteome by the covalent attachment of chemical groups or proteins to diverse cellular protein targets. These modifications include cysteine oxidation, glycosylation, ubiquitination, sumoylation, and neddylation, and influence ...

Post-translational modifications (PTMs) increase the functional diversity of the proteome by the covalent attachment of chemical groups or proteins to diverse cellular protein targets. These modifications include cysteine oxidation, glycosylation, ubiquitination, sumoylation, and neddylation, and influence virtually all aspects of cell biology. Further, targeted proteolysis via the ubiquitin proteasome system and selective autophagy maintains protein homeostasis and is increasingly identified at various compartmentalized sites within the cell (the endoplasmic reticulum, mitochondria, and ribosome). Dysregulation of PTMs and protein quality control have unique effects in heart disease and failure, and the underlying mechanisms remain elusive. Identification of molecular strategies targeting these modifications and improving protein quality control may offer novel avenues for the treatment of these yet incurable diseases.

In this Research Topic, we welcome original research and reviews related to protein modifications and quality control in cardiac health and disease on the following sub-topics:

1) PTMs in cardiac development and disease;
2) Protein quality control in human cardiomyopathy;
3) Targeting of ER stress signaling for the treatment of cardiomyopathy;
4) Mitophagy mechanisms and roles in cardiomyopathy.


Keywords: protein quality control, ubiquitin, ubiquitin-like proteins, autophagy, cardiomyopathy


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