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Studies show what stressed cells need to recover

Memphis, Tennessee, June 24, 2021

Colorful image of a cell up close.

Stress granule disassembly as seen from the vantage point of a viewer standing on the endoplasmic reticulum. VCP (green) is pulling G3BP1 (orange) out of a stress granule (blue) in a process mediated by ubiquitination. Credit: Michael P. Hughes, PhD, St. Jude Cell and Molecular Biology.

Cells must respond to changes in their environment that cause stress. They respond by either triggering cell death or adapting until the stress is removed.

To adapt to stress, cells can shut down key processes. They also form structures called stress granules. Stress granule regulation has been linked to neurodegenerative disease. Scientists at St. Jude are learning more about how stress granules are disassembled once stress passes.

The work shows that the same process that tags proteins so that the cells know to destroy them is also involved in how cells recover from stress. The process is called ubiquitination.

The team created a vast dataset about protein modification and regulation. They used the details to study a protein called G3BP1. The work showed that G3BP1 is a key component of the process that leads to disassembly of stress granules.

“We want to understand cell stress responses, from a basic cell biology perspective, but also because the processes are relevant to the biology of neurodegenerative diseases,” said J. Paul Taylor, MD, PhD, Cell and Molecular Biology Department chair and Howard Hughes Medical Institute investigator.

Science published two papers on this work.

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