title: SUMO conjugation - a mechanistic view.
abstract: The regulation of protein fate by modification with the small ubiquitin-related modifier (SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly dynamic due to the opposing activities of SUMO conjugation and SUMO deconjugation. SUMO conjugation is performed by the hierarchical action of E1, E2 and E3 enzymes, while its deconjugation involves SUMO-specific proteases. In this review, we summarize and compare the mechanistic principles of how SUMO gets conjugated to its substrate. We focus on the interplay of the E1, E2 and E3 enzymes and discuss how specificity could be achieved given the limited number of conjugating enzymes and the thousands of substrates.
authors.affiliation: Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
authors.forename: Andrea
authors.initials: A
authors.lastname: Pichler
authors.affiliation: Max Planck Institute of Immunobiology and Epigenetics, Department of Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
authors.forename: Chronis
authors.initials: C
authors.lastname: Fatouros
authors.affiliation: Max Planck Institute of Immunobiology and Epigenetics, Department of Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
authors.forename: Heekyoung
authors.initials: H
authors.lastname: Lee
authors.affiliation: Max Planck Institute of Immunobiology and Epigenetics, Department of Epigenetics, Stübeweg 51, D-79108 Freiburg, Germany.
authors.forename: Nathalie
authors.initials: N
authors.lastname: Eisenhardt
mesh_terms: D025842:SUMO-1 Protein / Q000378:metabolism; D013379:Substrate Specificity; D058207:Sumoylation; D025801:Ubiquitin / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism
chemical_list: D025842:SUMO-1 Protein; D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases