Another Route To Protein Disposal | Chemical & Engineering News
Volume 93 Issue 16 | p. 25 | Concentrates
Issue Date: April 20, 2015

Another Route To Protein Disposal

Proteasome Research: The protein called DJ-1 plays a role in regulating non-ubiquitin-dependent protein disposal
Department: Science & Technology | Collection: Life Sciences
News Channels: Biological SCENE
Keywords: proteasome, protein degradation, disposal

In the primary pathway for discarding proteins, cells tag targeted proteins with ubiquitin and deliver them to the proteasome, the cell’s garbage disposal. But there’s another protein disposal pathway that doesn’t involve ubiquitin and that uses only the central core of the proteasome, a portion called the 20S proteasome. Biologists previously thought this second pathway was a passive, unregulated process. Michal Sharon and coworkers of Israel’s Weizmann Institute of Science now report that the process is regulated at least in part by a Parkinson’s disease-related protein called DJ-1, which is in tissues throughout the human body (Nat. Commun. 2015, DOI: 10.1038/ncomms7609). The researchers found that DJ-1 both inhibits and indirectly activates protein degradation. It inhibits protein degradation by directly binding to the 20S proteasome. But during oxidative stress, DJ-1 activates a protein called Nrf2, which is itself an activator of the 20S proteasome. Sharon and coworkers are now studying where DJ-1 binds the proteasome to figure out the mechanism by which it exerts its effects.

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THREE MECHANISMS
The protein DJ-1 (yellow) could regulate the 20S proteasome (blue) by plugging its channel (left), blocking a recognition site (center), or acting allosterically at a remote site (right).
Credit: Courtesy of Michal Sharon
Images of the three possible ways in which DJ-1 (yellow) might regulate the 20S proteasome (blue).
 
THREE MECHANISMS
The protein DJ-1 (yellow) could regulate the 20S proteasome (blue) by plugging its channel (left), blocking a recognition site (center), or acting allosterically at a remote site (right).
Credit: Courtesy of Michal Sharon
 
Chemical & Engineering News
ISSN 0009-2347
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