Review
Nature Reviews Immunology 5, 941-952 (December 2005) | doi:10.1038/nri1731
Immunity by ubiquitylation: a reversible process of modification
Yun-Cai Liu1, Josef Penninger2 & Michael Karin3 About the authors
Abstract
The conjugation of ubiquitin, a 76-amino-acid peptide, to a protein substrate provides a tag that either marks the labelled protein for degradation or modulates its function. The process of protein ubiquitylation — which is catalysed by coordinated enzymatic reactions that are mediated by enzymes known as E1, E2 and E3 — has an important role in the modulation of immune responses. Importantly, protein ubiquitylation is a reversible process, and removal of ubiquitin molecules is mediated by de-ubiquitylating enzymes: for example, A20, which has been implicated in the regulation of immune responses. In addition, the conjugation of ubiquitin-like molecules, such as ISG15 (interferon-stimulated protein of 15 kDa), to proteins is also involved in immune regulation. This Review covers recent progress in our understanding of protein ubiquitylation in the immune system.
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Author affiliations
- Division of Cell Biology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121, USA.
- Institute for Molecular Biotechnology of the Austrian Academy of Sciences, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
- Laboratory of Gene Regulation and Signal Transduction, Department of Pharmacology, School of Medicine, University of California at San Diego, La Jolla, California 92093, USA.
Correspondence to: Yun-Cai Liu1 Email: yuncail@liai.org
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