Title

SUMOylation

Authors

Oliver Kerscher

Document Type

Article

Department/Program

Biology

Journal Title

eLS

Pub Date

2-15-2016

Publisher

Wiley

Place of Publication

Chichester

Journal Article URL

https://onlinelibrary.wiley.com/doi/pdf/10.1002/9780470015902.a0021849.pub2

Abstract

Eukaryotic cells utilise the dynamic addition and removal of SUMO, a small ubiquitin‐like modifier (UBL), to modulate protein functions, interactions and localisation. Protein SUMOylation involves a cascade of dedicated enzymes that facilitate the covalent modification of specific lysine residues on target proteins with monomers or polymers of SUMO. The cellular homeostasis of SUMOylated proteins is also regulated by SUMO proteases and SUMO‐targeted ubiquitin ligase (STUbLs). SUMO proteases cleave SUMO from modified proteins. In contrast, STUbLs ubiquitinate proteins modified with SUMO chains. Recent data suggests that ubiquitination via STUbLs effects the turnover of SUMOylated proteins as well as the spatio‐temporal composition of complexes that contain SUMO‐modified proteins. Defects in the controlled addition, removal and turnover of SUMO‐modified proteins greatly affect cellular fitness and contribute to developmental defects, cancer and protein aggregation disorders.

DOI

https://doi.org/10.1002/9780470015902.a0021849.pub2

Publisher Statement

This is the peer reviewed version of the following article:

Kerscher, O. (2016). SUMOylation. In eLS, John Wiley & Sons, Ltd (Ed.). doi:10.1002/9780470015902.a0021849.pub2, which has been published in final form at https://doi.org/10.1002/9780470015902.a0021849.pub2. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving

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