Stowers researchers create new framework for protein aggregation under acute stress

Patients with Parkinson’s disease, cardiovascular disease, and cystic fibrosis may have something in common - cells in their disease-affected tissues may produce misfolded proteins that are incapable of functioning normally. Stowers Institute scientists in the Rong Li Lab have studied where the misfolded proteins clump together in a cell, and how the cell can prevent the passage of these defective molecules to its daughter cell.

Investigator Rong Li, PhD, who headed the study, explains that her group has identified the quality control mechanism that limits the spreading of the misfolded protein aggregates to the daughter cell in a budding yeast model. During the mitosis stage of budding yeast’s division, aggregates of abnormal protein are tethered to well-anchored mitochondria in the mother cell. The mitochondria acquired by the bud, which will become the daughter cell, are largely free of the abnormal aggregates. As a result, the daughter cell does not inherit the defective proteins that burden the mother cell.

By identifying the quality control mechanisms that normally operate in cells, Li and other scientists are providing information that may prove relevant to treating disorders characterized by misfolded proteins.

These results were reported in the October 16, 2014, online issue of the journal Cell.