PXD015573

PXD015573 is an original dataset announced via ProteomeXchange.

Title	Proteome solubility changes under different proteostasis stresses
Description	The accumulation of aberrant protein aggregates in neurodegenerative diseases is associated with a widespread failure of the protein homeostasis system. To investigate whether there is a subproteome that consistently aggregates under stress and define the broader determinants for protein aggregation at the proteome level we measured the changes in proteome solubility of a mouse neuroblastoma cell line (Neuro2a) under 6 different protein homeostasis stresses, including a Huntington’s disease model, Hsp70, Hsp90, proteasome and ER-mediated folding inhibition, and oxidative stress. By partitioning cell lysates into supernatants and pellets by centrifugation, we found that just over a one-quarter of the proteome extensively changed in solubility upon one or more stresses. Surprisingly, almost all the increases in insolubility were counteracted by increases on solubility of other proteins. Each stress directed a highly specific pattern of change, which reflected the remodelling of protein complexes involved in adaptation to perturbation, most notably stress granule proteins, which were highly enriched but responded differently across the different 2 stresses. The solubility patterns clustered into molecular functions anticipated from stress responses and metabolic pathway hotspots, and indicate a robust rewiring of protein-ligand interactions.
HostingRepository	PRIDE
AnnounceDate	2020-01-29
AnnouncementXML	Submission_2020-01-29_02:00:32.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Xiaojing Sui
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2019-09-25 02:01:22	ID requested
⏵ 1	2020-01-29 02:00:33	announced

Sui X, Pires DEV, Ormsby AR, Cox D, Nie S, Vecchi G, Vendruscolo M, Ascher DB, Reid GE, Hatters DM, Widespread remodeling of proteome solubility in response to different protein homeostasis stresses. Proc Natl Acad Sci U S A, 117(5):2422-2431(2020) [pubmed]

ProteomeXchange project tag: Protein Misfolding and Aggregation (B/D-HPP), Biology/Disease-Driven Human Proteome Project (B/D-HPP), Human Proteome Project

submitter keyword: Protein homeostasis, protein aggregation, protein misfolding, Huntington’s disease, molecular chaperones, protein misfolding, metabolism, nuclear pore, aggregomics, stress granule formation, Hsp70, Hsp90, proteasome, ER-mediated folding inhibition, oxidative stress

Daniel Martin Hatters
contact affiliation	Department of Biochemistry and Molecular Biology; and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, VIC 3010. Australia
contact email	dhatters@unimelb.edu.au
lab head
Xiaojing Sui
contact affiliation	Bio21 Institute
contact email	suix@student.unimelb.edu.au
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD015573
     1. Label: PRIDE project
     2. Name: Proteome solubility changes under different proteostasis stresses