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Nat Commun. 2020 Feb 11;11(1):834. doi: 10.1038/s41467-020-14581-w.

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

Author information

1
Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Québec, Canada.
2
Molecular Biology Program, Université de Montréal, Montréal, Canada.
3
Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec, Canada.
4
Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Québec, Canada. pierre.thibault@umontreal.ca.
5
Department of Chemistry, Université de Montréal, Montréal, Québec, Canada. pierre.thibault@umontreal.ca.
6
Department of Biochemistry and Molecular Medicine, Université de Montréal, Montréal, Québec, Canada. pierre.thibault@umontreal.ca.

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.

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