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Cardiovascular Research Advance Access first published online on August 20, 2009
This version [Corrected Proof] published online on September 16, 2009
Cardiovascular Research, doi:10.1093/cvr/cvp287
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Published on behalf of the European Society of Cardiology. All rights reserved. © The Author 2009. For permissions please email: journals.permissions@oxfordjournals.org.

The ubiquitin–proteasome system in cardiac proteinopathy: a quality control perspective

Huabo Su and Xuejun Wang*

Division of Basic Biomedical Sciences, Sanford School of Medicine of the University of South Dakota, Lee Medical Building, 414 E. Clark Street, Vermillion, SD 57069, USA

* Corresponding author. Tel: +1 605 677 5132; Fax: +1 605 677 6381. E-mail address: xuejun.wang{at}usd.edu

Protein quality control (PQC) depends on elegant collaboration between molecular chaperones and targeted proteolysis in the cell. The latter is primarily carried out by the ubiquitin–proteasome system, but recent advances in this area of research suggest a supplementary role for the autophagy-lysosomal pathway in PQC-related proteolysis. The (patho)physiological significance of PQC in the heart is best illustrated in cardiac proteinopathy, which belongs to a family of cardiac diseases caused by expression of aggregation-prone proteins in cardiomyocytes. Cardiac proteasome functional insufficiency (PFI) is best studied in desmin-related cardiomyopathy, a bona fide cardiac proteinopathy. Emerging evidence suggests that many common forms of cardiomyopathy may belong to proteinopathy. This review focuses on examining current evidence, as it relates to the hypothesis that PFI impairs PQC in cardiomyocytes and contributes to the progression of cardiac proteinopathies to heart failure.

KEYWORDS Protein quality control; Ubiquitin; Proteasome; Desmin-related cardiomyopathy; Chaperone; Autophagy

Time for primary review: 44 days

This article is part of the Spotlight Issue on: The Role of the Ubiquitin-Proteasome Pathway in Cardiovascular Disease


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