Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy
Open Access
- 22 January 2007
- journal article
- review article
- Published by Portland Press Ltd. in Biochemical Society Transactions
- Vol. 35 (1) , 12-17
- https://doi.org/10.1042/bst0350012
Abstract
This review focuses on recent insights into the mechanisms and the biological functions of the proteasome. This large ATP-dependent proteolytic complex is the main site for protein degradation in mammalian cells and catalyses the rapid degradation of ubiquitinated proteins, and is the source of most antigenic peptides used by the immune system to screen for viruses and cancer. ATP is required to unfold globular proteins to open the gated channel into the 20S proteasome and to facilitate protein translation into it. Inhibitors of its proteolytic activity are widely used as research tools and have proven effective in cancer therapy.Keywords
This publication has 30 references indexed in Scilit:
- Nobel Committee Tags Ubiquitin for DistinctionNeuron, 2005
- Proteolysis: from the lysosome to ubiquitin and the proteasomeNature Reviews Molecular Cell Biology, 2005
- THE UBIQUITIN SYSTEMAnnual Review of Biochemistry, 1998
- PROTEASES AND THEIR TARGETS IN ESCHERICHIA COLIAnnual Review of Genetics, 1996
- ATP serves two distinct roles in protein degradation in reticulocytes, one requiring and one independent of ubiquitin.The Journal of cell biology, 1983
- The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La.Proceedings of the National Academy of Sciences, 1981
- A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes.Proceedings of the National Academy of Sciences, 1977
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- Intracellular Protein Degradation in Mammalian and Bacterial CellsAnnual Review of Biochemistry, 1974
- Degradation of Abnormal Proteins in Escherichia coliProceedings of the National Academy of Sciences, 1972