Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects
Date
2014
Authors
Scheffner, M.
Kumar, S.
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Journal article
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Biochimica et Biophysica Acta - Molecular Cell Research, 2014; 1843(1):61-74
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Martin Scheffner, Sharad Kumar
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Abstract
Members of the HECT family of E3 ubiquitin-protein ligases are characterized by a C-terminal HECT domain that catalyzes the covalent attachment of ubiquitin to substrate proteins and by N-terminal extensions of variable length and domain architecture that determine the substrate spectrumof a respectiveHECT E3. Since their discovery in 1995, it has become clear that deregulation of distinct HECT E3s plays an eminent role in human disease or disease-related processes including cancer, cardiovascular and neurological disorders, viral infections, and immune response. Thus, a detailed understanding of the structure–function aspects of HECT E3s aswell as the identification and characterization of the substrates and regulators of HECT E3s is critical in developing new approaches in the treatment of respective diseases. In this review, we summarize what is currently known about mammalian HECT E3s, with a focus on their biological functions and roles in pathophysiology.This article is part of a Special Issue entitled: Ubiquitin–Proteasome System
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© 2013 Elsevier B.V. All rights reserved.