title: Concepts in sumoylation: a decade on.
abstract: A decade has passed since SUMO (small ubiquitin-related modifier) was discovered to be a reversible post-translational protein modifier. During this time many enzymes that participate in regulated SUMO-conjugation and -deconjugation pathways have been identified and characterized. In parallel, the search for SUMO substrates has produced a long list of targets, which appear to be involved in most cellular functions. Sumoylation is a highly dynamic process and its outcomes are extremely diverse, ranging from changes in localization to altered activity and, in some cases, stability of the modified protein. At first glance, these effects have nothing in common; however, it seems that they all result from changes in the molecular interactions of the sumoylated proteins.
authors.affiliation: Department of Biochemie I, Faculty of Medicine, University of Goettingen, Humboldt Allee 23, 37073 Goettingen, Germany.
authors.forename: Ruth
authors.initials: R
authors.lastname: Geiss-Friedlander
authors.forename: Frauke
authors.initials: F
authors.lastname: Melchior
mesh_terms: D000818:Animals; D006801:Humans; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins; D025841:Small Ubiquitin-Related Modifier Proteins