PXD011483

PXD011483 is an original dataset announced via ProteomeXchange.

Title	Protein disaggregation by HSP101
Description	Proteins that are vital to cell survival can become unfolded during heat stress, leading to the formation of toxic aggregates. Molecular chaperones, proteases and autophagic pathways are required to protect cells from the accumulation of protein aggregates. Small Heat Shock Proteins (sHSPs) form a first line of defense by binding to unfolding proteins to prevent irreversible protein aggregation and the complex is rapidly sequestered in stress granules during heat stress recovery. HSP101 subsequently accumulates on the surface of these insoluble foci to mediate protein disaggregation. The dynamics of this process is consistent between different cell types but indicates that protein homeostasis varies particularly between shoot and root cells. Immunoblot analysis revealed that a substantial portion of proteins present in these foci have ubiquitin moieties and protein disaggregation is necessary prior to proteasomal degradation. Co-immuno precipitation of HSP101 revealed an interaction with the 26S proteasome and localization studies revealed that HSP101 and RPN1 (Proteasome regulatory particle) initially accumulate in distinct cytosolic foci during heat stress but co-localize in the same foci during heat stress recovery which could spatiotemporal facilitate the degradation of the aggregated ubiquitinated proteins. To determine which proteins are degraded by the proteasome after disaggregation, we catalogued 620 proteins that are resolubilized by HSP101 during heat stress recovery. GO-annotation analysis revealed a significant enrichment for RNA-binding proteins, UBC13-MMS2 complex, transcription factors and ubiquitin-protein ligases. None of these proteins were preferentially targeted by the proteasome, indicating that ubiquitination occurs on a broad range of proteins and is important for the clearance of a diverse array of proteins.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:49:55.650.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Fionn McLoughlin
SpeciesList	scientific name: Arabidopsis thaliana (Mouse-ear cress); NCBI TaxID: 3702;
ModificationList	ubiquitination signature dipeptidyl lysine; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-10-26 03:37:36	ID requested
1	2019-05-14 01:38:55	announced
2	2019-06-14 02:37:00	announced	Updated publication reference for PubMed record(s): 31113833.
⏵ 3	2024-10-22 04:49:59	announced	2024-10-22: Updated project metadata.

McLoughlin F, Kim M, Marshall RS, Vierstra RD, Vierling E, HSP101 Interacts with the Proteasome and Promotes the Clearance of Ubiquitylated Protein Aggregates. Plant Physiol, 180(4):1829-1847(2019) [pubmed]

10.1104/pp.19.00263;

submitter keyword: Arabidopsis, insoluble proteins

Elizabeth Vierling
contact affiliation	University of Massachussetts Amherst
contact email	vierling@biochem.umass.edu
lab head
Fionn McLoughlin
contact affiliation	Washington University in Saint Louis
contact email	fmcloughlin@wustl.edu
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/05/PXD011483

PRIDE project URI

• PRIDE
  1. PXD011483
     1. Label: PRIDE project
     2. Name: Protein disaggregation by HSP101