SUMO-SIM interactions: From structure to biological functions

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...

Full description

Saved in:
Bibliographic Details
Published in:Seminars in cell & developmental biology 2022-12, Vol.132, p.193-202
Main Authors: Lascorz, Jara, Codina-Fabra, Joan, Reverter, David, Torres-Rosell, Jordi
Format: Article
Language:English
Subjects:
E3 ligase
Protein Processing, Post-Translational
protein-protein interaction
Small Ubiquitin-Related Modifier Proteins - chemistry
Small Ubiquitin-Related Modifier Proteins - genetics
Small Ubiquitin-Related Modifier Proteins - metabolism
SUMO
SUMO interacting motif
Sumoylation
ubiquitin
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1084-9521
1096-3634
DOI:10.1016/j.semcdb.2021.11.007