title: SUMOylation and De-SUMOylation: wrestling with life's processes.
abstract: The small ubiquitin-like modifier (SUMO) is a ubiquitin-like protein that covalently modifies a large number of cellular proteins. SUMO modification has emerged as an important regulatory mechanism for protein function and localization. SUMOylation is a dynamic process that is mediated by activating (E1), conjugating (E2), and ligating (E3) enzymes and readily reversed by a family of ubiquitin-like protein-specific proteases (Ulp) in yeast and sentrin/SUMO-specific proteases (SENP) in human. This review will focus on the de-SUMOylating enzymes with special attention to their biological function.
authors.affiliation: Department of Cardiology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030, USA. etyeh@mdanderson.org
authors.forename: Edward T H
authors.initials: ET
authors.lastname: Yeh
mesh_terms: D000818:Animals; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism; D006801:Humans; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D021381:Protein Transport / Q000502:physiology; D025842:SUMO-1 Protein / Q000235:genetics / Q000378:metabolism*; D015003:Yeasts / Q000378:metabolism
chemical_list: D025842:SUMO-1 Protein; D003546:Cysteine Endopeptidases; C118083:Ulp1 protease