The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions.

Kolhe, Janhavi A; Babu, Neethu L; Freeman, Brian C

Kolhe, Janhavi A; Babu, Neethu L; Freeman, Brian C.

Affiliation

Kolhe JA; Department of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL, USA.
Babu NL; Department of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL, USA.
Freeman BC; Department of Cell and Developmental Biology, School of Molecular and Cellular Biology, University of Illinois-Urbana-Champaign, Urbana, IL, USA. Electronic address: bfree@illinois.edu.

Mol Cell ; 83(12): 2035-2044.e7, 2023 Jun 15.

Article in En | MEDLINE | ID: mdl-37295430

Subject(s)

Intrinsically Disordered Proteins; Molecular Chaperones; Proteome; Humans; HSP90 Heat-Shock Proteins/genetics; HSP90 Heat-Shock Proteins/metabolism; Molecular Chaperones/genetics; Molecular Chaperones/metabolism; Proteome/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Intrinsically Disordered Proteins/metabolism

Key words

Hsp90; fidelity of translation initiation; intrinsically disordered regions; molecular chaperone; proteostasis

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Full text: 1 Database: MEDLINE Main subject: Molecular Chaperones / Proteome / Intrinsically Disordered Proteins Limits: Humans Language: En Journal: Mol Cell Journal subject: BIOLOGIA MOLECULAR Year: 2023 Type: Article Affiliation country: United States

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