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Cardiovascular Research Advance Access first published online on July 25, 2009
This version [Corrected Proof] published online on August 11, 2009
Cardiovascular Research, doi:10.1093/cvr/cvp255
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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.

Stressing the ubiquitin/proteasome system

Nico P. Dantuma* and Kristina Lindsten*

Department of Cell and Molecular Biology, Karolinska Institutet, von Eulers väg 3 S-17177, Stockholm, Sweden

* Corresponding author. Tel: +46 852487384, Fax: +46 8313529, Email: nico.dantuma{at}ki.se (N.P.D.); kristina.lindsten{at}ki.se (K.L.)

Unfolded and misfolded proteins are inherently toxic to cells and have to be quickly and efficiently eliminated before they intoxicate the intracellular environment. This is of particular importance during proteotoxic stress when, as a consequence of intrinsic or extrinsic factors, the levels of misfolded proteins are transiently or persistently elevated. To meet this demand, metazoan cells have developed specific protein quality control mechanisms that allow the identification and proper handling of non-native proteins. An important defence mechanism is the specific destruction of these proteins by the ubiquitin/proteasome system (UPS). A number of studies have shown that various proteotoxic stress conditions can cause functional impairment of the UPS resulting in cellular dysfunction and apoptosis. In this review, we will summarize our current understanding of proteotoxic stress-induced dysfunction of the UPS and some of its implications for human pathologies.

KEYWORDS Ubiquitin; Proteasome; Proteotoxic stress; Conformational diseases; Ubiquitylation; Deubiquitylation

Time for primary review: 12 days

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


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