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Biochim Biophys Acta. 2014 Jan;1843(1):13-25. doi: 10.1016/j.bbamcr.2013.08.012. Epub 2013 Aug 27.

Regulation of proteasome activity in health and disease.

Author information

1
Albert Einstein College of Medicine, Department of Biochemistry, 1300 Morris Park Avenue, Bronx, NY 10461, USA. Electronic address: marion.schmidt@einstein.yu.edu.

Abstract

The ubiquitin-proteasome system (UPS) is the primary selective degradation system in the nuclei and cytoplasm of eukaryotic cells, required for the turnover of myriad soluble proteins. The hundreds of factors that comprise the UPS include an enzymatic cascade that tags proteins for degradation via the covalent attachment of a poly-ubiquitin chain, and a large multimeric enzyme that degrades ubiquitinated proteins, the proteasome. Protein degradation by the UPS regulates many pathways and is a crucial component of the cellular proteostasis network. Dysfunction of the ubiquitination machinery or the proteolytic activity of the proteasome is associated with numerous human diseases. In this review we discuss the contributions of the proteasome to human pathology, describe mechanisms that regulate the proteolytic capacity of the proteasome, and discuss strategies to modulate proteasome function as a therapeutic approach to ameliorate diseases associated with altered UPS function. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.

KEYWORDS:

Proteasome; Protein degradation; Ubiquitin

PMID:
23994620
PMCID:
PMC3858528
DOI:
10.1016/j.bbamcr.2013.08.012
[Indexed for MEDLINE]
Free PMC Article
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