title: Assays for investigating deSUMOylation enzymes.
abstract: Post-translational modifications by the SUMO (Small Ubiquitin-like MOdifier) family of proteins are recently discovered essential regulatory mechanisms. All SUMO proteins are synthesized as larger precursors that are matured by SUMO-specific proteases, known as SENPs, which remove several C-terminal amino acids of SUMO to expose the Gly-Gly motif. SENPs also remove SUMO modifications from target proteins, making this modification highly dynamic. At least six deSUMOylation enzymes, all of which are encoded by essential genes, have been identified in mammals. SENP1 has been shown to play an important role in the development of prostate cancer and in angiogenesis. This unit describes and discusses methods for characterizing the deSUMOylation enzymes. These assays enable the identification of inhibitors of these enzymes and investigation of their mechanism of inhibition in order to develop research tools and future therapeutics.
authors.affiliation: Department of Molecular Medicine, Beckman Research Institute of the City of Hope, Duarte, California, USA.
authors.forename: Ikenna G
authors.initials: IG
authors.lastname: Madu
authors.forename: Yuan
authors.initials: Y
authors.lastname: Chen
mesh_terms: D000818:Animals; D010450:Endopeptidases / Q000032:analysis* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D057075:Enzyme Assays / Q000379:methods*; D031541:Fluorescence Resonance Energy Transfer / 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; D010450:Endopeptidases