Researchers Discover a New Way to Control Cellular Protein Degradation

Researchers at the University of California, Berkeley, have developed a new strategy called stimulated protein degradation (SPD) that activates the cell's natural machinery to remove multiple unwanted proteins. The approach could open new possibilities for research into mitochondrial dysfunction and neurodegenerative diseases.

Cells use enzymes called E3 ubiquitin ligases to identify and mark unwanted proteins for degradation. Researchers focused on an enzyme called CUL2-FEM1B, which is inhibited by proteins known as BEX. By screening approximately 120,000 compounds, scientists identified molecules that displace BEX proteins and activate the enzyme. This allows CUL2-FEM1B to increase the degradation of multiple naturally recognized protein targets.

Experiments using human stem cell-derived neuronal models demonstrated improved mitochondrial protein import, energy production, and neuronal survival. The approach showed promising results in cellular models of COX deficiency syndrome and Friedreich's ataxia. The findings suggest that activating natural protein degradation pathways could provide an alternative to conventional targeted protein degradation, which generally focuses on individual proteins. However, further research is necessary to establish its safety and effectiveness in living organisms and humans.

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