Molecular shredders: how proteasomes fulfill their role |
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| Authors: | Groll Michael Clausen Tim |
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| Affiliation: | 1. Department of Oncology, The First Affiliated Hospital of Kunming Medical University, Kunming, Yunnan 650032, China;2. Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Kunming, Yunnan 650223, China;3. Chemotherapy Research Center, Yunnan Provincial Tumor Hospital, Kunming Medical University, Kunming, China;4. Department of Gastroenterology, The First Affiliated Hospital of Kunming Medical University, Kunming, Yunnan 650032, China;5. Kunming College of Life Science, University of Chinese Academy of Sciences, Kunming, Yunnan 650204, China |
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| Abstract: | The 20S proteasome is a large, cylinder-shaped protease that is found in all domains of life and plays a crucial role in cellular protein turnover. It has multiple catalytic centers located within the hollow cavity of a molecular cage. This architecture prevents unwanted degradation of endogenous proteins and promotes processive degradation of substrates by restricting the dissociation of partially digested polypeptides. Although this kind of self-compartmentalization is generally conserved, the proteasomes of bacteria, archaea and eukaryotes show many differences in architecture, subunit composition and regulation. The structure of the 20S proteasome and its inherent role in the regulation of proteasome function are gradually being elucidated. |
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