Journal
MOLECULAR GENETICS AND METABOLISM
Volume 77, Issue 1-2, Pages 44-56Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S1096-7192(02)00146-4
Keywords
ubiquitin; proteolysis; ubiquitin ligase; therapeutics; human disease
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Protein degradation is one of the tactics employed by the cell for irreversibly inactivating proteins. In eukaryotes, ATP-dependent protein degradation in the cytoplasm and nucleus is carried out by the 26S proteasome. Most proteins are targeted to the 26S proteasome by covalent attachment of a multi-ubiquitin chain. A key component of the enzyme cascade that results in attachment of the multi-ubiquitin chain to the target or labile protein is the ubiquitin ligase that controls the specificity of the ubiquitination reaction. Defects in ubiquitin-dependent proteolysis have been shown to result in a variety of human diseases, including cancer, neurodegenerative diseases, and metabolic disorders. This review focuses on the role of ubiquitin-dependent degradation in human disease and potential clinical applications that are being developed to exploit the cells natural proteolytic machinery to treat diseases. (C) 2002 Published by Elsevier Science (USA).
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