PXD011932-3

PXD011932 is an original dataset announced via ProteomeXchange.

Title	Quantitative proteomics identifies novel PIAS1 protein substrates involved in cell migration and motility
Description	The Protein Inhibitor of Activated STAT 1 (PIAS1) is an E3 SUMO ligase that plays important roles in various cellular pathways, including STAT signaling, p53 pathway, and the steroid hormone signaling pathway. PIAS1 can SUMOylate PML (at Lys-65 and Lys-160) and PML-RARα promoting their ubiquitin-mediated degradation. Increasing evidence shows that PIAS1 is overexpressed in various human malignancies, such as prostate and lung cancers. To understand the mechanism of action of PIAS1, we developed a quantitative SUMO proteomic approach to identify potential substrates of PIAS1 in a system-wide manner. Our analyses enabled the profiling of 983 SUMO sites on 544 proteins, of which 204 SUMO sites on 123 proteins were identified as putative PIAS1 substrates. These substrates were found to be involved in different cellular processes, including transcriptional regulation, DNA binding and cytoskeleton dynamics. Further functional studies on Vimentin (VIM), a type III intermediate filament protein involved in cytoskeleton organization and cell motility, revealed that PIAS1 exerts its effects on cell migration and cell invasion through the SUMOylation of VIM at Lys-439 and Lys-445 residues. VIM SUMOylation was necessary for its dynamic disassembly, and cells expressing a non-SUMOylatable VIM mutant showed reduced levels of proliferation and migration. Our approach not only provides a novel strategy for the identification of E3 SUMO ligase substrates, but also yields valuable biological insights into the unsuspected role of PIAS1 and VIM SUMOylation on cell motility.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:26:24.059.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Francis McManus
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	ubiquitination signature dipeptidyl lysine; phosphorylated residue; sumoylated lysine; deaminated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2018-12-04 07:25:47	ID requested
1	2020-02-06 07:08:06	announced
2	2020-03-24 01:05:49	announced	2020-03-24: Updated publication reference for PubMed record(s): 32047143.
⏵ 3	2024-10-22 04:26:31	announced	2024-10-22: Updated project metadata.

Li C, McManus FP, Plutoni C, Pascariu CM, Nelson T, Alberici Delsin LE, Emery G, Thibault P, Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility. Nat Commun, 11(1):834(2020) [pubmed]

10.1038/s41467-020-14581-w;

curator keyword: Biological

submitter keyword: PIAS1, Vimentin, cell invasion,SUMOylation, quantitative proteomics

Pierre Thibault
contact affiliation	Institute for Research in Immunology and Cancer, Québec, Canada, University of Montréal, Department of Chemistry, Québec, Canada
contact email	pierre.thibault@umontreal.ca
lab head
Francis McManus
contact affiliation	University of Montreal
contact email	francispmcmanus@gmail.com
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/2020/02/PXD011932

PRIDE project URI

• PRIDE
  1. PXD011932
     1. Label: PRIDE project
     2. Name: Quantitative proteomics identifies novel PIAS1 protein substrates involved in cell migration and motility