title: Biochemical analysis of protein SUMOylation.
abstract: SUMOylation, the covalent attachment of Small Ubiquitin-like MOdifier (SUMO) polypeptides to other proteins, is among the most important post-translational modifications that regulate the functional properties of a large number of proteins. SUMOylation is broadly involved in cellular processes such as gene transcription, hormone response, signal transduction, DNA repair, and nuclear transport. SUMO modification has also been implicated in the pathogenesis of human diseases, such as cancer, neurodegenerative disorders, and viral infection. Attachment of a SUMO protein to another protein is carried out in multiple steps catalyzed by three enzymes. This unit describes and discusses the in vitro biochemical methods used for investigating each step of the SUMOylation process. In addition, a high-throughput screening protocol is included for the identification of inhibitors of SUMOylation.
authors.affiliation: Department of Molecular Medicine, Beckman Research Institute of the City of Hope, Duarte, California, USA.
authors.forename: Aileen Y
authors.initials: AY
authors.lastname: Alontaga
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Bobkova
authors.forename: Yuan
authors.initials: Y
authors.lastname: Chen
mesh_terms: D000818:Animals; D001671:Biochemistry / Q000379:methods*; D057166:High-Throughput Screening Assays / Q000379:methods*; D006801:Humans; D011506:Proteins / Q000378:metabolism*; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism; D058207:Sumoylation
chemical_list: D011506:Proteins; D025841:Small Ubiquitin-Related Modifier Proteins