Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in

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Studies on yeast prions have provided insight into the role of various cellular factors involved in amyloid based disorders. Among the various cellular components the chaperone network has emerged as a crucial regulator of formation and propagation of yeast prions. The chaperone machinery primarily consists of Hsp70 and Hsp90 families of proteins, whose activity is further modulated by multiple co-chaperones. Though it is known that Hsp70s and its co-factors influence prion strength and stability, the role of Hsp90 chaperone machinery in yeast prion propagation is not clear. Here we examine the role of Hsp90 chaperones and show that the C-terminal MEEVD motif on Hsp90, which is required for interaction with tetratricopeptide repeat domain containing co-chaperones, is crucial for propagation of the yeast prion [URE3]. Further study revealed a novel role of the Hsp90 co-chaperone Cpr7 in the propagation of infectious amyloid and thus broadens our understanding about the cellular role of immunophilins.

Vyšlo v časopise: Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in. PLoS Genet 11(10): e32767. doi:10.1371/journal.pgen.1005567
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1005567

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