Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells

Nikola Arsic, Tania Slatter, Gilles Gadea, Etienne Villain, Aurelie Fournet, Marina Kazantseva, Frédéric Allemand, Nathalie Sibille, Martial Seveno, Sylvain Rossi, Sunali Mehta, Serge Urbach, Jean-Christophe Bourdon, Pau Bernado, Andrey V. Kajava, Antony Braithwaite and Pierre Roux ()
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Nikola Arsic: Université de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237
Tania Slatter: University of Otago
Gilles Gadea: Université de la Réunion, Unité Mixte 134 Processus Infectieux en Milieu Insulaire Tropical, INSERM Unité 1187, CNRS Unité Mixte de Recherche 9192, IRD Unité Mixte de Recherche 249. Plateforme Technologique CYROI
Etienne Villain: Université de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237
Aurelie Fournet: Université de Montpellier
Marina Kazantseva: University of Otago
Frédéric Allemand: Université de Montpellier
Nathalie Sibille: Université de Montpellier
Martial Seveno: Université de Montpellier
Sylvain Rossi: MRI, UMS BioCampus Montpellier, CNRS, INSERM, Université de Montpellier
Sunali Mehta: University of Otago
Serge Urbach: Université de Montpellier
Jean-Christophe Bourdon: Dundee Cancer Centre, University of Dundee, Ninewells Hospital and Medical School
Pau Bernado: Université de Montpellier
Andrey V. Kajava: Université de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237
Antony Braithwaite: University of Otago
Pierre Roux: Université de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract The p53 isoform, Δ133p53β, is critical in promoting cancer. Here we report that Δ133p53β activity is regulated through an aggregation-dependent mechanism. Δ133p53β aggregates were observed in cancer cells and tumour biopsies. The Δ133p53β aggregation depends on association with interacting partners including p63 family members or the CCT chaperone complex. Depletion of the CCT complex promotes accumulation of Δ133p53β aggregates and loss of Δ133p53β dependent cancer cell invasion. In contrast, association with p63 family members recruits Δ133p53β from aggregates increasing its intracellular mobility. Our study reveals novel mechanisms of cancer progression for p53 isoforms which are regulated through sequestration in aggregates and recruitment upon association with specific partners like p63 isoforms or CCT chaperone complex, that critically influence cancer cell features like EMT, migration and invasion.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25550-2

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DOI: 10.1038/s41467-021-25550-2

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