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This article is part of the supplement: Ubiquitin-Proteasome System in Disease Part 1

Open Access Highly Accessed Review

HECT E3s and human disease

Martin Scheffner1* and Olivier Staub2

Author Affiliations

1 Department of Biology, University of Konstanz, 78457 Konstanz, Germany

2 Department of Pharmacology and Toxicology, University of Lausanne, Rue du Bugnon 27, 1005 Lausanne, Switzerland

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BMC Biochemistry 2007, 8(Suppl 1):S6  doi:10.1186/1471-2091-8-S1-S6

Published: 22 November 2007

Abstract

In a simplified view, members of the HECT E3 family have a modular structure consisting of the C-terminal HECT domain, which is catalytically involved in the attachment of ubiquitin to substrate proteins, and N-terminal extensions of variable length and sequence that mediate the substrate specificity of the respective HECT E3. Although the physiologically relevant substrates of most HECT E3s have remained elusive, it is becoming increasingly clear that HECT E3s play an important role in sporadic and hereditary human diseases including cancer, cardiovascular (Liddle's syndrome) and neurological (Angelman syndrome) disorders, and/or in disease-relevant processes including bone homeostasis, immune response and retroviral budding. Thus, molecular approaches to target the activity of distinct HECT E3s, regulators thereof, and/or of HECT E3 substrates could prove valuable in the treatment of the respective diseases.

Publication history: Republished from Current BioData's Targeted Proteins database (TPdb; http://www.targetedproteinsdb.com webcite).