PXD023841

PXD023841 is an original dataset announced via ProteomeXchange.

Title	SUMO Proteomics Analyses Identify Protein Inhibitor of Activated STAT-Mediated Regulatory Networks Involved in Cell Cycle and Cell Proliferation
Description	Protein inhibitor of activated STAT (PIAS) are E3 SUMO ligases playing important roles in protein stability and signaling transduction pathways. PIAS proteins are overexpressed in the triple-negative breast cancer cell line MDA-MB-231, and PIAS knockout (KO) results in a reduction in cell proliferation and cell arrest in S phase. However, the molecular mechanisms underlying PIAS functions in cell proliferation and cell cycle remain largely unknown. Here, we used quantitative SUMO proteomics to explore the regulatory role of PIAS SUMO E3 ligases upon CRISPR/Cas9 KO of individual PIAS. A total of 1422 sites were identified, and around 10% of SUMO sites were regulated following KO of one or more PIAS genes. We identified protein substrates that were either specific to individual PIAS ligase or regulated by several PIAS ligases. Ki-67 and TOP2A, which are involved in cell proliferation and epithelial-to-mesenchymal transition, are SUMOylated at several lysine residues by all PIAS ligases, suggesting a level of redundancy between these proteins. Confocal microscopy and biochemical experiments revealed that SUMOylation regulated TOP2A protein stability, while this modification is involved in the recruitment of Ki-67 nucleolar proteins containing SUMO interacting motif. These results provide novel insights into both the redundant and specific regulatory mechanisms of cell proliferation and cell cycle mediated by PIAS SUMO E3 ligases.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_07:30:32.813.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Chongyang Li
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	ubiquitination signature dipeptidyl lysine; sumoylated lysine; acetylated residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2021-01-26 23:12:00	ID requested
1	2023-02-02 09:05:28	announced
⏵ 2	2023-11-14 07:30:35	announced	2023-11-14: Updated project metadata.

Li C, Boutet A, Pascariu CM, Nelson T, Courcelles M, Wu Z, Comtois-Marotte S, Emery G, Thibault P, SUMO Proteomics Analyses Identify Protein Inhibitor of Activated STAT-Mediated Regulatory Networks Involved in Cell Cycle and Cell Proliferation. J Proteome Res, 22(3):812-825(2023) [pubmed]

submitter keyword: HEK293 SUMO3m LC-MS/MS PIAS SUMO E3 ligase proteomics

Pierre Thibault
contact affiliation	1 Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Québec, Canada. 2 Department of Chemistry, Université de Montréal, Montréal, Québec, Canada. 3 Department of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada.
contact email	pierre.thibault@umontreal.ca
lab head
Chongyang Li
contact affiliation	University of Montreal
contact email	chongyangwin@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD023841
     1. Label: PRIDE project
     2. Name: SUMO Proteomics Analyses Identify Protein Inhibitor of Activated STAT-Mediated Regulatory Networks Involved in Cell Cycle and Cell Proliferation