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

ABSTRACT: Molecular chaperones govern proteome health to support cell homeostasis. An essential eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology approach we characterized the features driving the Hsp90 physical interactome.

INSTRUMENT(S): MaxQuant

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Janhavi Kolhe

LAB HEAD: Brian Freeman

PROVIDER: PXD040875 | Pride | 2023-08-10

REPOSITORIES: pride

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	F120_R2.mzML	Mzml
	F120_R3.mzML	Mzml
	F325_R1.mzML	Mzml
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The Hsp90 molecular chaperone governs client proteins by targeting intrinsically disordered regions.

Kolhe Janhavi A JA Babu Neethu L NL Freeman Brian C BC

Molecular cell 20230608 12

Molecular chaperones govern proteome health to support cell homeostasis. An essential eukaryotic component of the chaperone system is Hsp90. Using a chemical-biology approach, we characterized the features driving the Hsp90 physical interactome. We found that Hsp90 associated with ∼20% of the yeast proteome using its three domains to preferentially target intrinsically disordered regions (IDRs) of client proteins. Hsp90 selectively utilized an IDR to regulate client activity as well as maintaine ...[more]

PMID: 37295430

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