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Article

An acetylation site in the middle domain of Hsp90 regulates chaperone function.

Molecular cell - 12 Jan 2007

Scroggins Bradley T, Robzyk Kenneth, Wang Dongxia, Marcu Monica G, Tsutsumi Shinji, Beebe Kristin, Cotter Robert J, Felts Sara, Toft David, Karnitz Larry, Rosen Neal, Neckers Len

Abstract excerpt

Heat-shock protein 90 (Hsp90) chaperones a key subset of signaling proteins and is necessary for malignant transformation. Hsp90 is subject to an array of posttranslational modifications that affect its function, including acetylation. Histone deacetylase (HDAC) inhibitors and knockdown of HDAC6 induce Hsp90 acetylation and inhibit its activity. However, direct determination of the functional consequences of...

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Share to Acetylation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to HSP90 Heat-Shock Proteins

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Source

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Identifiers

PMID: 17218278
DOI: 10.1016/j.molcel.2006.12.008
PMCID: PMC1839984

Genes

HDAC6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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