Breaking Down Aggregates: Chaperone Interplay Driving the Hsp70 Disaggregation Machinery

Speaker: dr Agnieszka Kłosowska, Laboratory of Evolutionary Biochemistry, Intercollegiate Faculty of Biotechnology UG & MUG

Talk:  Breaking Down Aggregates: Chaperone Interplay Driving the Hsp70 Disaggregation Machinery

Time: 19.06.2026, 09:00

Venue: Intercollegiate Faculty of Biotechnology, Abrahama 58, hall 042B

Accumulation of protein aggregates in cells is associated with stress, aging, and many diseases. In my research, I use biochemical methods to study protein quality control systems that prevent aggregation‑driven toxicity, with an emphasis on molecular chaperones capable of aggregate disassembly and the reactivation of misfolded proteins.

During my PhD at the Intercollegiate Faculty of Biotechnology UG & MUG, I described regulatory mechanisms that keep the yeast disaggregase Hsp104 active in aggregate clearance while limiting its potentially harmful unfolding activity. For my postdoctoral training, I joined Dan Tawfik’s laboratory at the Weizmann Institute of Science, where I examined how molecular chaperones influence the evolutionary trajectories of proteins with aggregation‑prone folds. After returning to Poland, I set out to understand how the human Hsp70 chaperone system—operating in the absence of Hsp104—solubilises stress‑induced aggregates as well as amyloid fibrils linked to neurodegeneration. Since 2025, I have been leading an NCN‑funded SONATA project exploring functional specialization among several proteins of the human Hsp70 family.

In my seminar, I will describe how cooperation between different chaperones at the aggregate surface leads to effective Hsp70‑dependent disaggregation.