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SUMO-SIM interactions: From structure to biological functions.
- Source :
-
Seminars in Cell & Developmental Biology . Dec2022, Vol. 132, p193-202. 10p. - Publication Year :
- 2022
-
Abstract
- 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10849521
- Volume :
- 132
- Database :
- Academic Search Index
- Journal :
- Seminars in Cell & Developmental Biology
- Publication Type :
- Academic Journal
- Accession number :
- 160251777
- Full Text :
- https://doi.org/10.1016/j.semcdb.2021.11.007