Matches in SemOpenAlex for { <https://semopenalex.org/work/W4283589786> ?p ?o ?g. }
- W4283589786 abstract "Alzheimer's disease is a neurodegenerative disorder in which misfolding and aggregation of pathologically modified Tau is critical for neuronal dysfunction and degeneration. The two central chaperones Hsp70 and Hsp90 coordinate protein homeostasis, but the nature of the interaction of Tau with the Hsp70/Hsp90 machinery has remained enigmatic. Here we show that Tau is a high-affinity substrate of the human Hsp70/Hsp90 machinery. Complex formation involves extensive intermolecular contacts, blocks Tau aggregation and depends on Tau's aggregation-prone repeat region. The Hsp90 co-chaperone p23 directly binds Tau and stabilizes the multichaperone/substrate complex, whereas the E3 ubiquitin-protein ligase CHIP efficiently disassembles the machinery targeting Tau to proteasomal degradation. Because phosphorylated Tau binds the Hsp70/Hsp90 machinery but is not recognized by Hsp90 alone, the data establish the Hsp70/Hsp90 multichaperone complex as a critical regulator of Tau in neurodegenerative diseases." @default.
- W4283589786 created "2022-06-28" @default.
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- W4283589786 date "2022-06-27" @default.
- W4283589786 modified "2023-10-14" @default.
- W4283589786 title "Hsp multichaperone complex buffers pathologically modified Tau" @default.
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- W4283589786 doi "https://doi.org/10.1038/s41467-022-31396-z" @default.
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