The Logic of the 26S Proteasome

The ubiquitin proteasome pathway is responsible for most of the protein degradation in mammalian cells. Rates of degradation by this pathway have generally been assumed to be determined by rates of ubiquitylation. However, recent studies indicate that proteasome function is also tightly regulated an...

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Bibliographic Details
Published in:Cell 2017-05, Vol.169 (5), p.792-806
Main Authors: Collins, Galen Andrew, Goldberg, Alfred L.
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Allosteric Regulation
Animals
Eukaryota - chemistry
Eukaryota - metabolism
Humans
Phosphorylation
Proteasome Endopeptidase Complex - chemistry
Proteasome Endopeptidase Complex - metabolism
proteasome phosphorylation
protein degradation
protein turnover
Proteolysis
ubiquitin proteasome system
Ubiquitination
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Summary:The ubiquitin proteasome pathway is responsible for most of the protein degradation in mammalian cells. Rates of degradation by this pathway have generally been assumed to be determined by rates of ubiquitylation. However, recent studies indicate that proteasome function is also tightly regulated and determines whether a ubiquitylated protein is destroyed or deubiquitylated and survives longer. This article reviews recent advances in our understanding of the proteasome's multistep ATP-dependent mechanism, its biochemical and structural features that ensure efficient proteolysis and ubiquitin recycling while preventing nonselective proteolysis, and the regulation of proteasome activity by interacting proteins and subunit modifications, especially phosphorylation. The proteasome is responsible for most protein degradation in mammalian cells. Recent advances in the field now provide a greater understanding of its mode of action and regulation.
ISSN:0092-8674
1097-4172
DOI:10.1016/j.cell.2017.04.023