SUMO conjugation – a mechanistic view-Reference-Cited by-同舟云学术

SUMO conjugation – a mechanistic view

Published:2017-03-01 Issue:1 Volume:8 Page:13-36
ISSN:1868-503X
Container-title:Biomolecular Concepts
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Author:

Pichler Andrea¹,Fatouros Chronis²,Lee Heekyoung²,Eisenhardt Nathalie²

Affiliation:

1. 1Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany

2. 2Max Planck Institute of Immunobiology and Epigenetics, Department of Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany

Abstract

AbstractThe regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly dynamic due to the opposing activities of SUMO conjugation and SUMO deconjugation. SUMO conjugation is performed by the hierarchical action of E1, E2 and E3 enzymes, while its deconjugation involves SUMO-specific proteases. In this review, we summarize and compare the mechanistic principles of how SUMO gets conjugated to its substrate. We focus on the interplay of the E1, E2 and E3 enzymes and discuss how specificity could be achieved given the limited number of conjugating enzymes and the thousands of substrates.

Publisher

Walter de Gruyter GmbH

Subject

Cellular and Molecular Neuroscience,General Biochemistry, Genetics and Molecular Biology,General Medicine

Link

https://www.degruyter.com/downloadpdf/journals/bmc/8/1/article-p13.xml

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