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Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts
Author(s) -
Celen Arda B.,
Sahin Umut
Publication year - 2020
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15319
Subject(s) - sumo protein , ubiquitin , regulator , sumo enzymes , gene isoform , computational biology , biology , posttranslational modification , microbiology and biotechnology , lysine , genetics , biochemistry , gene , amino acid , enzyme
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.