The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation

Despite the key proposed function of Hop/Stip1/Sti1 for protein folding and maturation, it is not essential in a number of eukaryotes and bacteria lack an ortholog. Didier Picard’s group has explored why Hop is present in eukaryotes, what its critical functions are, and whether and how the eukaryotic Hsp70-Hsp90 molecular chaperone machines may function without Hop to ensure proteostasis. Their studies on the functions of Hop as a co-chaperone of the Hsp70-Hsp90 molecular chaperone machines led them to the discovery of alternative cellular strategies that ensure proper protein folding and proteostasis in human and yeast cells lacking this co-chaperone. These findings highlight the persistence of evolutionarily more ancient mechanisms in eukaryotic cells that may contribute to balance protein folding and degradation under certain conditions.

This study was published in Nature Communications on November 25th 2020.

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