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Review
. 2020 Aug;287(15):3110-3140.
doi: 10.1111/febs.15319. Epub 2020 May 1.

Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts

Arda B Celen  1 , Umut Sahin  1
Affiliations
Free article
Review

Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts

Arda B Celen et al. FEBS J. 2020 Aug.
Free article

Abstract

Sumoylation is an essential post-translational modification intimately involved in a diverse range of eukaryotic cellular mechanisms. Small ubiquitin-like modifier (SUMO) protein isoforms can be reversibly linked to lysine residues that reside within specific motifs on thousands of target substrates, leading to modulations in stability, solubility, localization, and interactor profile. Since its initial discovery almost 25 years ago, SUMO has been described as a key regulator of genomic stability, cell proliferation, and infection among other processes. In this review, we trace the exciting developments in the history of this critical modifier, highlighting SUMO's roles in pathogenesis as well as its potential for the development of targeted therapies for numerous diseases.

Keywords: PML nuclear bodies; PML/RARα oncogene; SUMO; cancer; cross-talk; degradation; neurodegeneration; post-translational modification; proteasome; ubiquitin.

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