ArticleThe journal of physical chemistry letters2026
Post-Translational Modification as an Allosteric Switch in Hsp90: How Dual Phosphorylation Locks Chaperone Complexes into Hyperstabilized States.
Giorgio Bonollo, Benedetto Roncati, Luca Torielli, Shujuan Wang, Chiranjeevi Pasala, Silvia Pavoni, Francesco Frigerio, Fabrizio Cinquini, Gabriela Chiosis, Stefano A Serapian and 1 more
Abstract read
In one paragraphArticle in The journal of physical chemistry letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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What it found
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2 · The registryThe trial behind it
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3 · Its place in the literatureWho cites it
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4 · The recordCorrections and comments
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5 · Who and what moneyAuthors and funding
11 authors.
Giorgio BonolloDepartment of Chemistry, University of Pavia, Via Taramelli 12, 27100, Pavia, Italy.
Benedetto RoncatiDepartment of Chemistry, University of Pavia, Via Taramelli 12, 27100, Pavia, Italy.
Shujuan WangChemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065, United States.ORCID 0000-0003-1341-5777 Chiranjeevi PasalaChemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065, United States.ORCID 0000-0001-5612-6241 Silvia PavoniDepartment of Physical Chemistry, R&D EniSpA, Via Felice Maritano 26, 20097 San Donato Milanese (Mi), Italy.
Francesco FrigerioDepartment of Physical Chemistry, R&D EniSpA, Via Felice Maritano 26, 20097 San Donato Milanese (Mi), Italy.
Fabrizio CinquiniDepartment of Physical Chemistry, R&D EniSpA, Via Felice Maritano 26, 20097 San Donato Milanese (Mi), Italy.
Gabriela ChiosisChemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065, United States.
Stefano A SerapianDepartment of Chemistry, University of Pavia, Via Taramelli 12, 27100, Pavia, Italy.ORCID 0000-0003-0122-8499 Funding
X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SELWYN M VICKERS · 1985 to 2026
$347.4MImpact of sex differences on the trajectory of interactome dysfunctions across the AD spectrumR01AG074004 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA, GINSBERG, STEPHEN D · 2021 to 2025
$6.0MChaperome networks in Alzheimer's diseaseR01AG067598 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI ARANCIO, OTTAVIO, CHIOSIS, GABRIELA · 2021 to 2025
$5.9MSelective interactome vulnerability across the Alzheimer’s disease spectrumR01AG072599 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI GABRIELA CHIOSIS, STEPHEN D GINSBERG · 2023 to 2026
$5.4M[18F]-PU-AD epichaperome PET imaging probeRF1AG071805 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA, DUNPHY, MARK P. · 2022 to 2025
$4.8MSmall molecule Hsp90 inhibitors in AD treatmentU01AG032969 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA · 2010 to 2014
$3.5MA chemical chaperomics platform for ADR56AG061869 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA · 2018 to 2019
$1.8MSelective interactome vulnerability across the Alzheimer’s disease spectrumR56AG072599 · NIA · SLOAN-KETTERING INST CAN RESEARCH · PI CHIOSIS, GABRIELA, GINSBERG, STEPHEN D · 2021 to 2021
$1.2MNCI NIH HHS P30 CA008748NIA NIH HHS R01 AG067598NIA NIH HHS R01 AG072599NIA NIH HHS R01 AG074004NIA NIH HHS R56 AG061869NIA NIH HHS R56 AG072599NIA NIH HHS RF1 AG071805NIA NIH HHS U01 AG032969
6 · The paper itselfAbstract
Multimicrosecond MD simulations reveal that dual phosphorylation at Ser226/Ser255 of Hsp90β acts as a molecular clamp, rigidifying the overall structure, propagating allosteric coordination changes to distal domains, and stabilizing cochaperone-client interfaces. These findings provide an atomistic mechanism by which post-translational modifications can stabilize Hsp90 interaction states that are compatible with epichaperome formation, with implications for disease biology and therapeutic targeting.
Indexed as
HSP90 Heat-Shock ProteinsMolecular ChaperonesProtein Processing, Post-TranslationalAllosteric RegulationMolecular Dynamics SimulationPhosphorylationHSP90 Heat-Shock ProteinsMolecular Chaperones
Identifiers
PMID42410314
PMCPMC13383824
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