Molecular chaperones promote correct protein folding and counteract aggregation. We lack a systematic understanding of which of these molecular chaperones are relevant for proteins that aggregate in neurodegenerative diseases. Several neurodegenerative diseases, including Huntington's disease, involve aggregation of proteins with expanded polyglutamine regions. Using an unbiased CRISPR screen, we found that the co-chaperone DNAJC7 acts as a suppressor of polyglutamine aggregation in human cells.
This work was led by Dr. Biswarathan Ramani, first as a postdoc in the Kampmann lab, and then in his independent lab.
See here for the publication:
Ramani B, Ehsani K, Kampmann M (2026) The Hsp40 cochaperone DNAJC7 regulates polyglutamine aggregation and exhibits context-dependent effects on polyglycine aggregation. Journal of Biological Chemistry 302(4):111292.