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Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation

Epichaperomes are chaperone assemblies that reorganize protein networks under stress. Here, authors reveal how HSP90 phosphorylation drives epichaperome formation, linking this process to cancer cell behaviors and pluripotent stem cell functions.

Tanaya Roychowdhury
Seth W. McNutt
Feixia Chu
ResearchOpen Access16 Oct 2024
Nature Communications

Volume: 15, P: 1-28
Causative role of PDLIM2 epigenetic repression in lung cancer and therapeutic resistance

PDLIM2 is repressed epigenetically in lung cancers, which are frequently resistant to anti-PD-1/PD-L1 and chemotherapy. Here, the authors describe the mechanism through which epigenetic restoration of PDLIM2 synergises with anti-PD-1 and chemotherapy in lung cancers.

Fan Sun
Liwen Li
Zhaoxia Qu
ResearchOpen Access22 Nov 2019
Nature Communications

Volume: 10, P: 1-13
Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2

Specific inhibitors against Hsp90 paralogs show that Hsp90 and Grp94 regulate HER2 in a cell-specific and proteome alteration-driven manner.

Pallav D Patel
Pengrong Yan
Gabriela Chiosis
Research01 Sept 2013
Nature Chemical Biology

Volume: 9, P: 677-684
The epichaperome is an integrated chaperome network that facilitates tumour survival

Chaperomes are dynamic assemblies of proteins that regulate cellular homeostasis but specific cellular stresses remodel chaperome components into a stable chaperome network called the epichaperome, which might offer a new cancer target.

Anna Rodina
Tai Wang
Gabriela Chiosis
Research05 Oct 2016
Nature

Volume: 538, P: 397-401
Systems-level analyses of protein-protein interaction network dysfunctions via epichaperomics identify cancer-specific mechanisms of stress adaptation

Epichaperomics allow the study of protein-protein interactions and their alterations, but probes have been limited to capturing HSP90 epichaperomes. Here, the authors introduce and validate a toolset of HSP70 epichaperome ligands, and use them in epichaperomics to identify a mechanism with which cancer cells can enhance the fitness of mitotic protein networks.

Anna Rodina
Chao Xu
Gabriela Chiosis
ResearchOpen Access23 Jun 2023
Nature Communications

Volume: 14, P: 1-26
The epichaperome is a mediator of toxic hippocampal stress and leads to protein connectivity-based dysfunction

The biology of Alzheimer’s disease (AD) remains unknown. We propose AD is a protein connectivity-based dysfunction disorder whereby a switch of the chaperome into epichaperomes rewires proteome-wide connectivity, leading to brain circuitry malfunction that can be corrected by novel therapeutics.

Maria Carmen Inda
Suhasini Joshi
Gabriela Chiosis
ResearchOpen Access16 Jan 2020
Nature Communications

Volume: 11, P: 1-19
Chemical tools for epichaperome-mediated interactome dysfunctions of the central nervous system

Here, the authors show structural, biochemical, and functional insights into the discovery of epichaperome‐ directed chemical probes for use in central nervous system diseases. Probes emerging from this work have translated to human clinical studies in Alzheimer’s disease and cancer.

Alexander Bolaender
Danuta Zatorska
Gabriela Chiosis
ResearchOpen Access03 Aug 2021
Nature Communications

Volume: 12, P: 1-19
Reply to ‘H-STS, L-STS and KRJ-I are not authentic GEPNET cell lines’

Mariano J. Alvarez
Pengrong Yan
Andrea Califano
Correspondence23 Sept 2019
Nature Genetics

Volume: 51, P: 1427-1428
Hsp90 inhibition results in autophagy-mediated proteasome-independent degradation of IκB kinase (IKK)

Guoliang Qing
Pengrong Yan
Gutian Xiao
Research07 Nov 2006
Cell Research

Volume: 16, P: 895-901
Pharmacologically controlling protein-protein interactions through epichaperomes for therapeutic vulnerability in cancer

Joshi, Gomes et al. employ a chemical modulation approach of the cellular interactome to a hyperconnectivity state and show association with the increased response of pancreatic cancer cell lines to specific drugs, including those that target the MAPK-pathways and PI3K-mTOR pathway. To achieve this, the authors employ chemical modulation of the interactome via epichaperome inhibition with the small molecule PU-H71.

Suhasini Joshi
Erica DaGama Gomes
Gabriela Chiosis
ResearchOpen Access25 Nov 2021
Communications Biology

Volume: 4, P: 1-20
Hsp90 regulates processing of NF-κB2 p100 involving protection of NF-κB-inducing kinase (NIK) from autophagy-mediated degradation

Guoliang Qing
Pengrong Yan
Gutian Xiao
Research12 Jun 2007
Cell Research

Volume: 17, P: 520-530

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