Protein alteration controls cell's response to stress, immunity and lifespan

phys.org | 1/15/2019 | Staff
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Scientists have revealed a key mechanism in worms that is involved in controlling the cell's response to stress, a study in eLife reports.

The discovery provides crucial new insights into a stress-response mechanism called unfolded protein response (UPR) and will help researchers understand the processes that protect cells, boost immunity and extend lifespan.

Ability - Organism - Environment - Ability - Stress

The ability of an organism to cope with an ever-changing and challenging environment lies in its ability to activate stress responses. One of the most important biological components affected by stress are the mitochondria—the energy-producing machinery of our cells. Animals respond to mitochondrial stress by activating the UPR—a surveillance program that monitors mitochondrial function and signals to the nucleus (the control centre of the cell) - if something is wrong. Although some components of the UPR have been identified, exactly how it is controlled is still unclear.

"We had previously identified genes that are important for the activation of the mitochondrial stress response," explains lead author Kaiyu Gao, graduate student at the Institute of Molecular Medicine, Peking University, China. "Among these was the ulp-4 gene, which is an enzyme that removes a molecule called SUMO from proteins, dramatically affecting their function. In this study, we set out to see whether the ULP-4 enzyme was necessary for the stress response, and whether it influenced this response by removing SUMO groups."

Team - Activity - Gene - Worms - UPR

The team first blocked the activity of the ulp-4 gene in worms and looked at whether this affected the UPR response. This prevented the stress response in mitochondria but not stress responses in other parts of the cell. When they restored high levels of the ULP-4...
(Excerpt) Read more at: phys.org
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