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PXD011932 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleQuantitative proteomics identifies novel PIAS1 protein substrates involved in cell migration and motility
DescriptionThe 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.
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFrancis McManus
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListubiquitination signature dipeptidyl lysine; phosphorylated residue; sumoylated lysine; deaminated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive HF; Orbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02018-12-04 07:25:47ID requested
12020-02-06 07:08:06announced
22020-03-24 01:05:49announced2020-03-24: Updated publication reference for PubMed record(s): 32047143.
Publication List
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]
Keyword List
curator keyword: Biological
submitter keyword: SUMOylation, PIAS1, Vimentin, cell invasion, quantitative proteomics
Contact List
Pierre Thibault
contact affiliationInstitute for Research in Immunology and Cancer, Québec, Canada, University of Montréal, Department of Chemistry, Québec, Canada
contact emailpierre.thibault@umontreal.ca
lab head
Francis McManus
contact affiliationUniversity of Montreal
contact emailfrancispmcmanus@gmail.com
dataset submitter
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