Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts.
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.
['Celen|Arda B|AB|', 'Sahin|Umut|U|0000-0002-4100-5751']
D000846:Anniversaries and Special Events D006801:Humans D007239:Infections D009369:Neoplasms D019636:Neurodegenerative Diseases D011499:Protein Processing, Post-Translational D025841:Small Ubiquitin-Related Modifier Proteins D058207:Sumoylation
post-translational modification SUMO PML nuclear bodies PML/RARα oncogene cancer cross-talk degradation neurodegeneration proteasome ubiquitin