E3 Ubiquitin Ligases: From Structure to Physiology

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Editorial

26 November 2020

Editorial: E3 Ubiquitin Ligases: From Structure to Physiology

Julien D. F. Licchesi

,

Heike Laman

,

Fumiyo Ikeda

and

Victor M. Bolanos-Garcia

3,910 views

2 citations

Editors

4

Victor M Bolanos-Garcia

Oxford Brookes University

Julien Licchesi

University of Bath

Heike Laman

University of Cambridge

Fumiyo Ikeda

Osaka University

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This Research Topic is part of the E3 Ubiquitin Ligases series:
E3 Ubiquitin Ligases: From Structure to Physiology to Therapeutics, Volume II

Ubiquitin ligases refers to a family of proteins that are widely distributed in animals and plants and act as key regulators of cell metabolism and cell signaling. Recent reviews nicely describe our current understanding of the function of specific classes of ubiquitin ligases. However, a more holistic account of ubiquitin ligases in health and disease remain as an important pending assignment in the field.

This Research Topic addresses this gap in knowledge and aims to include contributions from leading scientists with a long-standing interest in ubiquitin ligases, ranging from the study of the function and structure of HECT-type, RNA-binding, SCF, E1, and E3 ubiquitin ligase; alternative Ubiquitin-modification Pathways; Cullin-RING ubiquitin ligase complex, to the discovery of inhibitors and activators of RING and U-box type E3 Ligases; and the role of ubiquitin ligases in autophagy and of ubiquitin-modifying enzymes in the regulation of the immune response.

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Editors

Victor M Bolanos-Garcia

Oxford Brookes University

Julien Licchesi

University of Bath

Heike Laman

University of Cambridge

Fumiyo Ikeda

Osaka University

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142,484 Total views

108,724 Article views

30,864 Article downloads

2,896 Topic views

Published In

Frontiers in Physiology

Integrative Physiology

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