New Study Reveals Mechanism of Action of Protein Clump-Dissolving Chaperone

Toxicity associated with misfolded proteins is characteristic of many neurodegenerative diseases including ALS (See Nov 2011 news story), and avenues to selectively dissolve protein aggregates or preemptively inhibit their formation are being explored for therapeutic purposes (see June 2013 conference news). A new study from the laboratory of James Shorter at the University of Pennsylvania in Philadelphia reveals the structural basis for the diverse functions of heat shock protein 104 (Hsp104), a yeast chaperone that dissolves protein aggregates. Shorter and colleagues have been engineering variants of Hsp104 that could potentially be administered to humans (see Aug 2014 news story), and the new findings, published January 22 in Molecular Cell online, could dramatically expedite progress in that direction.

Click here to read more about the mechanism through which Hsp104 dissolves both disorganized protein aggregates and prions.

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