Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation

• Published in: Circulation research Vol. 100; no. 9; pp. 1276 - 1291
• Main Authors: Herrmann, Joerg, Lerman, Lilach O, Lerman, Amir
• Format: Journal Article
• Language: English
• Published: Hagerstown, MD American Heart Association, Inc 11.05.2007; Lippincott
• Subjects: Animals; Autophagy-Related Protein 12; Biological and medical sciences; Cardiovascular Diseases - etiology; Cytokines - physiology; DNA Repair; Fundamental and applied biological sciences. Psychology; Humans; NEDD8 Protein; Proteasome Endopeptidase Complex - physiology; Proteins - metabolism; Proteins - physiology; Ribosomal Proteins - physiology; Signal Transduction; Small Ubiquitin-Related Modifier Proteins - physiology; SUMO-1 Protein - physiology; Ubiquitin - physiology; Ubiquitins - physiology; Vertebrates: cardiovascular system; Ubiquitin; Vertebrata; Mammalia; Cell cycle; ubiquitin-like proteins; Inflammation; Circulatory system; Metabolism; Protein
• ISSN: 0009-7330; 1524-4571
• DOI: 10.1161/01.RES.0000264500.11888.f0

The discovery of the ubiquitin system was awarded with the Nobel Prize in Chemistry in 2004. Labeling of intracellular proteins for degradation by a multienzymatic complex, called the proteasome, was identified as the main function of this system. Subsequently, it was discovered that the attachment of ubiquitin to proteins can modify their function without degradation. Finally, a number of other molecules were recognized to be conjugated to proteins in a manner similar to ubiquitin and were henceforth called ubiquitin-like proteins. This review provides an overview of this class of molecules and its implication for function, subcellular location, and half-life of proteins.