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

Author

Listed:
  • Chongyang Li

    (Université de Montréal
    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
    Université de Montréal)

  • Lara Elis Alberici Delsin

    (Université de Montréal
    Université de Montréal)

  • Gregory Emery

    (Université de Montréal
    Université de Montréal)

  • Pierre Thibault

    (Université de Montréal
    Université de Montréal
    Université de Montréal)

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.

Suggested Citation

  • Chongyang Li & Francis P. McManus & Cédric Plutoni & Cristina Mirela Pascariu & Trent Nelson & Lara Elis Alberici Delsin & Gregory Emery & Pierre Thibault, 2020. "Quantitative SUMO proteomics identifies PIAS1 substrates involved in cell migration and motility," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14581-w
    DOI: 10.1038/s41467-020-14581-w
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    Cited by:

    1. Shouheng Jin & Xing He & Ling Ma & Zhen Zhuang & Yiliang Wang & Meng Lin & Sihui Cai & Lu Wei & Zheyu Wang & Zhiyao Zhao & Yaoxing Wu & Lin Sun & Chunwei Li & Weihong Xie & Yong Zhao & Zhou Songyang &, 2022. "Suppression of ACE2 SUMOylation protects against SARS-CoV-2 infection through TOLLIP-mediated selective autophagy," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Dan Tan & Meiping Lu & Yuqing Cai & Weibo Qi & Fugen Wu & Hangyang Bao & Meiyu Qv & Qiangqiang He & Yana Xu & Xiangzhi Wang & Tingyu Shen & Jiahao Luo & Yangxun He & Junsong Wu & Lanfang Tang & Muhamm, 2023. "SUMOylation of Rho-associated protein kinase 2 induces goblet cell metaplasia in allergic airways," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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