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Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility
Chongyang Li1,2, Francis P McManus1, Cédric Plutoni1
1Institute for Research in Immunology and Cancer, Université de Montréal, Montréal, Québec, Canada.
Nature Communications
|February 13, 2020
Summary
Protein inhibitor of activated STAT1 (PIAS1), a SUMO ligase, is linked to cancer. This study identifies PIAS1 substrates, revealing its role in vimentin SUMOylation and cell migration.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- The protein inhibitor of activated STAT1 (PIAS1) functions as an E3 SUMO ligase, implicated in critical cellular processes.
- Overexpression of PIAS1 is observed in several human cancers, such as prostate and lung malignancies.
Purpose of the Study:
- To systematically identify substrates of PIAS1 using quantitative SUMO proteomics.
- To investigate the role of PIAS1 and its substrates in cellular functions, particularly cell motility.
Main Methods:
- Quantitative SUMO proteomics was employed to identify PIAS1 substrates across the proteome.
- Specific SUMOylation sites on vimentin (VIM) by PIAS1 were determined.
- The functional impact of VIM SUMOylation on cell migration was assessed using a non-SUMOylatable mutant.
Main Results:
- The study identified 983 SUMO sites on 544 proteins, designating 62 as putative PIAS1 substrates.
- Vimentin (VIM) was identified as a PIAS1 substrate, with SUMOylation occurring at Lys-439 and Lys-445.
- VIM SUMOylation was found to be essential for its dynamic disassembly, and its absence reduced cell migration.
Conclusions:
- This research provides a method for identifying E3 SUMO ligase substrates.
- The findings highlight a previously unrecognized function of PIAS1 in regulating cell motility through vimentin SUMOylation.
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