What is it about?
Mitochondria rely on the protease ClpXP to break down damaged or misfolded proteins, ensuring proper mitochondrial function. ClpXP is particularly important for the survival of various cancer cells, including leukemia. This study investigates how a chemical modification known as serine phosphorylation regulates protein degradation by ClpXP. The researchers found that adding a phosphate group to the amino acid serine on specific proteins acts as a tag, signaling ClpXP to accelerate their breakdown.
Featured Image
Photo by Louis Reed on Unsplash
Why is it important?
This study is the first to uncover how human ClpXP breaks down proteins in mitochondria. Understanding how this protease selects and processes its target proteins provides new insights that could help develop treatments targeting ClpXP, particularly for cancer.
Perspectives
The cytoplasm is well-known for its elegant Ubiquitin-Proteasome System, which carefully marks proteins for degradation. In contrast, mitochondria—membrane-bound organelles—have their own distinct system for breaking down proteins. This study advances our understanding of how mitochondrial proteases degrade proteins independently of the cytoplasmic machinery.
Yue Feng
University of Toronto
Read the Original
This page is a summary of: Serine phosphorylation facilitates protein degradation by the human mitochondrial ClpXP protease, Proceedings of the National Academy of Sciences, January 2025, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2422447122.
You can read the full text:
Contributors
The following have contributed to this page
