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Researchers from the Verstreken lab (VIB-KU Leuven) have identified a completely novel function for Hsp90, one of the most common and most studied proteins in our body. In addition to its well-known role as a protein chaperone, Hsp90 stimulates exosome release. These findings shed new light on treatment strategies for both cancer and neurodegenerative diseases.

Hsp90, short for heat-shock protein 90, is one of the most abundant proteins, making up one or two out of every hundred proteins in our cells. Heat shock proteins are conserved across animals, plants and even fungi. Their name dates back to the ’80, when they were first described as a group of proteins upregulated upon sudden heat stress.

Over the past decades we have learned an awful lot about Hsp90’s function. As a protein chaperone, it assists in the proper folding of other proteins and stabilizes them in case of cellular stress. Hsp90 also helps degrade damaged or misfolded proteins that are beyond salvation. These myriad functions make Hsp90 a crucial governor of protein homeostasis in the cell. Membrane deformation and exosome release

New research by prof. Patrik Verstreken and his team at VIB and KU Leuven shows that–independently of its chaperone function–Hsp90

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