Ubiquitin-like proteins: new wines in new bottles.
Ubiquitin is a small polypeptide that covalently modifies other cellular proteins and targets them to the proteasome for degradation. In recent years, ubiquitin-dependent proteolysis has been demonstrated to play a critical role in the regulation of many cellular processes, such as cell cycle progression, cell signaling, and immune recognition. The recent discovery of three new ubiquitin-like proteins, NEDD8, Sentrin/SUMO, and Apg12, has further broadened the horizon of this type of post-translational protein modification. This review will focus on the biology and biochemistry of the Sentrin/SUMO and NEDD8 modification pathways, which are clearly distinct from the ubiquitination pathway and have unique biological functions.
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Divisions of Cardiology and Molecular Medicine, Medical School, and Research Center for Cardiovascular Diseases, Institute of Molecular Medicine for the Prevention of Human Diseases, The University of Texas-Houston Health Science Center, Houston, USA.
Gong
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Kamitani
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D000595:Amino Acid Sequence; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D000075687:NEDD8 Protein; D010447:Peptide Hydrolases; D011499:Protein Processing, Post-Translational; D025842:SUMO-1 Protein; D017386:Sequence Homology, Amino Acid; D014452:Ubiquitins / Q000235:genetics / Q000378:metabolism*
D000075687:NEDD8 Protein; C082860:NEDD8 protein, human; C513172:Nedd8 protein, mouse; D025842:SUMO-1 Protein; D014452:Ubiquitins; D010450:Endopeptidases; D010447:Peptide Hydrolases; C404512:SENP1 protein, human; D003546:Cysteine Endopeptidases; C492190:Senp3 protein, mouse