DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation.
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ABSTRACT:
SUBMITTER: Hou Z
PROVIDER: S-EPMC8429438 | biostudies-literature | 2021 Sep
REPOSITORIES: biostudies-literature
Publications
DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation.
Hou Zhiqiang Z Wydorski Pawel M PM Perez Valerie A VA Mendoza-Oliva Aydé A Ryder Bryan D BD Mirbaha Hilda H Kashmer Omar O Joachimiak Lukasz A LA
Nature communications 20210909 1
Molecular chaperones, including Hsp70/J-domain protein (JDP) families, play central roles in binding substrates to prevent their aggregation. How JDPs select different conformations of substrates remains poorly understood. Here, we report an interaction between the JDP DnaJC7 and tau that efficiently suppresses tau aggregation in vitro and in cells. DnaJC7 binds preferentially to natively folded wild-type tau, but disease-associated mutants in tau reduce chaperone binding affinity. We identify t ...[more]
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