Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation

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...

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Bibliographic Details
Published in:Circulation research 2007-05, Vol.100 (9), p.1276-1291
Main Authors: Herrmann, Joerg, Lerman, Lilach O, Lerman, Amir
Format: Article
Language:English
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
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Summary: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.
ISSN:0009-7330
1524-4571
DOI:10.1161/01.RES.0000264500.11888.f0