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

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

p53 isoform Δ133p53β is reported to promote intrinsic oncogenic functions. Here the authors show Δ133p53β is sequestered as aggregates in an inactive form, while association with interacting partners including p63 isoforms and the CCT chaperone complex promotes Δ133p53β activity, resulting in enhanc...

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Main Authors: Nikola Arsic, Tania Slatter, Gilles Gadea, Etienne Villain, Aurelie Fournet, Marina Kazantseva, Frédéric Allemand, Nathalie Sibille, Martial Seveno, Sylvain de Rossi, Sunali Mehta, Serge Urbach, Jean-Christophe Bourdon, Pau Bernado, Andrey V. Kajava, Antony Braithwaite, Pierre Roux
Format: Article
Language:English
Published: Nature Publishing Group 2021-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-25550-2
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spelling doaj-68225466d9dc4ec1bb5844837f0a0ec82021-09-19T11:48:27ZengNature Publishing GroupNature Communications2041-17232021-09-0112111810.1038/s41467-021-25550-2Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cellsNikola Arsic0Tania Slatter1Gilles Gadea2Etienne Villain3Aurelie Fournet4Marina Kazantseva5Frédéric Allemand6Nathalie Sibille7Martial Seveno8Sylvain de Rossi9Sunali Mehta10Serge Urbach11Jean-Christophe Bourdon12Pau Bernado13Andrey V. Kajava14Antony Braithwaite15Pierre Roux16Université de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237Department of Pathology, University of OtagoUniversité 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 CYROIUniversité de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237Université de MontpellierDepartment of Pathology, University of OtagoUniversité de MontpellierUniversité de MontpellierUniversité de MontpellierMRI, UMS BioCampus Montpellier, CNRS, INSERM, Université de MontpellierDepartment of Pathology, University of OtagoUniversité de MontpellierDundee Cancer Centre, University of Dundee, Ninewells Hospital and Medical SchoolUniversité de MontpellierUniversité de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237Department of Pathology, University of OtagoUniversité de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237p53 isoform Δ133p53β is reported to promote intrinsic oncogenic functions. Here the authors show Δ133p53β is sequestered as aggregates in an inactive form, while association with interacting partners including p63 isoforms and the CCT chaperone complex promotes Δ133p53β activity, resulting in enhanced cancer cell migration and invasion.https://doi.org/10.1038/s41467-021-25550-2
collection DOAJ
language English
format Article
sources DOAJ
author Nikola Arsic
Tania Slatter
Gilles Gadea
Etienne Villain
Aurelie Fournet
Marina Kazantseva
Frédéric Allemand
Nathalie Sibille
Martial Seveno
Sylvain de Rossi
Sunali Mehta
Serge Urbach
Jean-Christophe Bourdon
Pau Bernado
Andrey V. Kajava
Antony Braithwaite
Pierre Roux
spellingShingle Nikola Arsic
Tania Slatter
Gilles Gadea
Etienne Villain
Aurelie Fournet
Marina Kazantseva
Frédéric Allemand
Nathalie Sibille
Martial Seveno
Sylvain de Rossi
Sunali Mehta
Serge Urbach
Jean-Christophe Bourdon
Pau Bernado
Andrey V. Kajava
Antony Braithwaite
Pierre Roux
Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
Nature Communications
author_facet Nikola Arsic
Tania Slatter
Gilles Gadea
Etienne Villain
Aurelie Fournet
Marina Kazantseva
Frédéric Allemand
Nathalie Sibille
Martial Seveno
Sylvain de Rossi
Sunali Mehta
Serge Urbach
Jean-Christophe Bourdon
Pau Bernado
Andrey V. Kajava
Antony Braithwaite
Pierre Roux
author_sort Nikola Arsic
title Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
title_short Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
title_full Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
title_fullStr Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
title_full_unstemmed Δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
title_sort δ133p53β isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-09-01
description p53 isoform Δ133p53β is reported to promote intrinsic oncogenic functions. Here the authors show Δ133p53β is sequestered as aggregates in an inactive form, while association with interacting partners including p63 isoforms and the CCT chaperone complex promotes Δ133p53β activity, resulting in enhanced cancer cell migration and invasion.
url https://doi.org/10.1038/s41467-021-25550-2
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