Study describes how cells return to normal after responding to stress

rotein that is responsible for targeting chaperone substrates for degradation. The thinking is that when a protein is too damaged to be refolded, CHIP ubiquitinates that protein so that it can be degraded."

The results present a previously unknown mechanism for how the cell determines whether or not to degrade misfolded proteins or to degrade the heat shock proteins that have been produced so that it can then resume its physiologic activities.

"We think that the stress response is required to protect cells from damage during stress, but it is also important to let the cells return to the normal condition as soon as possible," said Dr. Shu-Bing Qian, postdoctoral researcher in the Patterson lab and first author of the study.

They found that during stress heat shock proteins attempt to refold proteins. And if unsuccessful, CHIP tags those proteins for degradation. Once all the proteins that have been tagged for degradation have been removed by the proteasome, a barrel-shaped complex of proteins that digests other proteins, CHIP begins to tag the heat shock proteins themselves for degradation. Once they are all removed, the cell can go back to business as usual.

Patterson's group has made mouse models lacking CHIP and has found that the mice are more susceptible to many different stressful circumstances, such as fever and heart attacks.

"That finding seems to be due to the accumulation of misfolded proteins," said Patterson. "Chronic dysregulation of the CHIP molecular pathway would also be expected to be maladaptive."

One hope is that this finding could be extended to human diseases where a faulty stress response has already been implicated.

Patterson said there are specific diseases in which chronic protein misfolding is critical, including neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's. "So we expect that CHIP would play an important role in cellular adaptation under those circumstances as wel

Contact: L.H. Lang
University of North Carolina School of Medicine

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