The Logic of the 26S Proteasome.

Cell

Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. Electronic address:

Published: May 2017

AI Article Synopsis

  • * New findings show that the proteasome itself plays a critical role in deciding whether a tagged protein gets destroyed or can survive longer, emphasizing its regulatory function.
  • * This article discusses advancements in understanding how the proteasome works, including its energy-dependent processes, structural features for efficient protein breakdown, and how its activity is modified by interacting proteins and phosphorylation.

Article Abstract

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.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5609836PMC
http://dx.doi.org/10.1016/j.cell.2017.04.023DOI Listing

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The Logic of the 26S Proteasome.

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