Structure and Function of the 26S Proteasome
| Autor: | Eric R. Greene, Andreas Martin, Ken C. Dong, Ellen A. Goodall, Erik Jonsson, Jared A.M. Bard |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Proteasome Endopeptidase Complex Saccharomyces cerevisiae Proteins Cell division Protein Conformation Regulator Protein degradation Models Biological Biochemistry Article Substrate Specificity 03 medical and health sciences 0302 clinical medicine Humans Deubiquitinating Enzymes Ubiquitin Chemistry Molecular Motor Proteins AAA proteins Cell biology 030104 developmental biology Proteasome Proteome ATPases Associated with Diverse Cellular Activities Signal transduction 030217 neurology & neurosurgery Deubiquitination |
| Zdroj: | Annual Review of Biochemistry. 87:697-724 |
| ISSN: | 1545-4509 0066-4154 |
| DOI: | 10.1146/annurev-biochem-062917-011931 |
| Popis: | As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The proteasome's cellular functions range from general protein homeostasis and stress response to the control of vital processes such as cell division and signal transduction. To reliably process all the proteins presented to it in the complex cellular environment, the proteasome must combine high promiscuity with exceptional substrate selectivity. Recent structural and biochemical studies have shed new light on the many steps involved in proteasomal substrate processing, including recognition, deubiquitination, and ATP-driven translocation and unfolding. In addition, these studies revealed a complex conformational landscape that ensures proper substrate selection before the proteasome commits to processive degradation. These advances in our understanding of the proteasome's intricate machinery set the stage for future studies on how the proteasome functions as a major regulator of the eukaryotic proteome. |
| Databáze: | OpenAIRE |
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