Minireviews
SUMOylation and De-SUMOylation: Wrestling with Life's Processes*

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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.

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The abbreviations used are: SUMO, small ubiquitin-like modifier; SENP, sentrin/SUMO-specific protease; siRNA, small interfering RNA; TNF, tumor necrosis factor; Epo, erythropoietin; VHL, von Hippel-Lindau.

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This is the third of three articles in the Thematic Minireview Series on Regulation of Signaling by Non-degradative Ubiquitination. This minireview will be reprinted in the 2009 Minireview Compendium, which will be available in January, 2010.