PXD050251-2

PXD050251 is an original dataset announced via ProteomeXchange.

Title	Phosphorylation-Driven Epichaperome Assembly: A Critical Regulator of Cellular Adaptability and Proliferation
Description	The intricate protein-chaperone network is vital for cellular function. Recent discoveries have unveiled the existence of specialized chaperone complexes called epichaperomes, protein assemblies orchestrating the reconfiguration of protein-protein interaction networks, enhancing cellular adaptability and proliferation. This study delves into the structural and regulatory aspects of epichaperomes, with a particular emphasis on the significance of post-translational modifications in shaping their formation and function. A central finding of this investigation is the identification of specific PTMs on HSP90, particularly at serine residues Ser226 and Ser255 situated within an intrinsically disordered region, as critical determinants in epichaperome assembly. Our data demonstrate that the phosphorylation of these serine residues enhances HSP90's interaction with other chaperones and co-chaperones, creating a microenvironment conducive to epichaperome formation. Furthermore, this study establishes a direct link between epichaperome function and cellular physiology, especially in contexts where robust proliferation and adaptive behavior are essential, such as cancer and stem cell maintenance. These findings not only provide mechanistic insights but also hold promise for the development of novel therapeutic strategies targeting chaperone complexes in diseases characterized by epichaperome dysregulation, bridging the gap between fundamental research and precision medicine.
HostingRepository	PRIDE
AnnounceDate	2024-10-18
AnnouncementXML	Submission_2024-10-18_01:01:14.208.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Feixia Chu
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	(R)-5-oxo-1; phosphorylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF; LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2024-02-29 17:11:50	ID requested
1	2024-10-17 09:11:46	announced
⏵ 2	2024-10-18 01:01:15	announced	2024-10-18: Updated project metadata.

10.1038/s41467-024-53178-5;

10.1038/S41467-024-53178-5;

Roychowdhury T, McNutt SW, Pasala C, Nguyen HT, Thornton DT, Sharma S, Botticelli L, Digwal CS, Joshi S, Yang N, Panchal P, Chakrabarty S, Bay S, Markov V, Kwong C, Lisanti J, Chung SY, Ginsberg SD, Yan P, De Stanchina E, Corben A, Modi S, Alpaugh ML, Colombo G, Erdjument-Bromage H, Neubert TA, Chalkley RJ, Baker PR, Burlingame AL, Rodina A, Chiosis G, Chu F, Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation. Nat Commun, 15(1):8912(2024) [pubmed]

submitter keyword: HSP90, posttranslational modifications, epichaperome

Feixia Chu, Gabriela Chiosis
contact affiliation	Department of Molecular, Cellular & Biomedical Sciences, University of New Hampshire, Durham, NH 03824, USA Chemical Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
contact email	feixia.chu@unh.edu
lab head
Feixia Chu
contact affiliation	University of New Hampshire
contact email	feixia.chu@unh.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD050251
     1. Label: PRIDE project
     2. Name: Phosphorylation-Driven Epichaperome Assembly: A Critical Regulator of Cellular Adaptability and Proliferation