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Article

Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.

Nature communications - 19 May 2026

Wan Chanjuan, Zhu Lei, Wang Simin, Zhang Xueqing, Zhao Jun, Qu Xiaozhan, Huang Chengdong

Abstract excerpt

Phosphorylation is a central post-translational mechanism for on-demand regulation of protein function. In the ATP-dependent molecular chaperone Hsp90, multiple phosphorylation sites have been implicated in activity control, yet how individual sites encode regulatory instructions remains unclear. Here, using solution NMR spectroscopy, we delineate how site-specific phosphorylation distinctly reshapes the...

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Identifiers

PMID: 42156390
DOI: 10.1038/s41467-026-73400-w
PMCID: PMC13381810

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

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