期刊
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
卷 132, 期 -, 页码 193-202出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2021.11.007
关键词
SUMO; SUMO interacting motif; ubiquitin; protein -protein interaction; E3 ligase
资金
- Ministerio de Ciencia, Innovacion y Universidades [PGC2018-097796-B-I00, 2017-SGR-569]
- AGAUR-Generalitat de Catalunya [PGC2018-098423-B-I00]
- Spanish government [FPU19/03526]
Post-translational modification by SUMO proteins involves non-covalent interactions with other proteins, which play crucial roles in regulating protein activity, localization, and stability.
Post-translational modification by Small Ubiquitin-like Modifier (SUMO) proteins regulates numerous cellular processes. This modification involves the covalent and reversible attachment of SUMO to target proteins through an isopeptide bond, using a cascade of E1, E2 and E3 SUMOylation enzymes. Most functions of SUMO depend on the establishment of non-covalent protein-protein interactions between SUMOylated substrates and their binding partners. The vast majority of these interactions involve a conserved surface in the SUMO protein and a SUMO interacting motif (SIM), a short stretch of hydrophobic amino acids and an acidic region, in the interactor protein. Despite single SUMO-SIM interactions are relatively weak, they can have a huge impact at different levels, altering the activity, localization and stability of proteins, triggering the formation of macromolecular assemblies or inducing phase separation. Moreover, SUMO-SIM interactions are ubiquitous in most enzymes of the SUMO pathway, and play essential roles in SUMO conjugation and deconjugation. Here, we analyze the role of SUMO-SIM contacts in SUMO enzymes and targets and discuss how this humble interaction participates in SUMOylation reactions and mediates the outcome of this essential post-translational modification.
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