Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility

Chongyang Li, Francis P. McManus, Cédric Plutoni, Cristina Mirela Pascariu, Trent Nelson, Lara Elis Alberici Delsin, Gregory Emery and Pierre Thibault ()
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Chongyang Li: Université de Montréal
Francis P. McManus: Université de Montréal
Cédric Plutoni: Université de Montréal
Cristina Mirela Pascariu: Université de Montréal
Trent Nelson: Université de Montréal
Lara Elis Alberici Delsin: Université de Montréal
Gregory Emery: Université de Montréal
Pierre Thibault: Université de Montréal

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: Abstract The protein inhibitor of activated STAT1 (PIAS1) is an E3 SUMO ligase that plays important roles in various cellular pathways. Increasing evidence shows that PIAS1 is overexpressed in various human malignancies, including prostate and lung cancers. Here we used quantitative SUMO proteomics to identify potential substrates of PIAS1 in a system-wide manner. We identified 983 SUMO sites on 544 proteins, of which 62 proteins were assigned as putative PIAS1 substrates. In particular, vimentin (VIM), a type III intermediate filament protein involved in cytoskeleton organization and cell motility, was SUMOylated by PIAS1 at Lys-439 and Lys-445 residues. VIM SUMOylation was necessary for its dynamic disassembly and cells expressing a non-SUMOylatable VIM mutant showed a reduced level of migration. Our approach not only enables 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.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14581-w

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DOI: 10.1038/s41467-020-14581-w

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