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

Authors
  • Arsic, Nikola1, 2
  • Slatter, Tania3
  • Gadea, Gilles4
  • Villain, Etienne1, 2
  • Fournet, Aurelie5, 2
  • Kazantseva, Marina3
  • Allemand, Frédéric5, 2
  • Sibille, Nathalie5, 2
  • Seveno, Martial6, 2
  • de Rossi, Sylvain7
  • Mehta, Sunali3
  • Urbach, Serge8, 2
  • Bourdon, Jean-Christophe9
  • Bernado, Pau5, 2
  • Kajava, Andrey V.1, 2, 10
  • Braithwaite, Antony3
  • Roux, Pierre1, 2
  • 1 Université de Montpellier, Centre de Recherche en Biologie Cellulaire de Montpellier (CRBM) CNRS, UMR 5237,
  • 2 Université de Montpellier,
  • 3 University of Otago,
  • 4 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, Sainte Clotilde, France
  • 5 Centre de Biochimie Structurale (CBS), INSERM, CNRS, 29 rue de Navacelles, Montpellier, France
  • 6 BioCampus Montpellier, CNRS, INSERM,
  • 7 MRI, UMS BioCampus Montpellier, CNRS, INSERM, Université de Montpellier,
  • 8 IGF, CNRS, INSERM, Montpellier, France
  • 9 Dundee Cancer Centre, University of Dundee, Ninewells Hospital and Medical School,
  • 10 Institut de Biologie Computationnelle,
Type
Published Article
Journal
Nature Communications
Publisher
Springer Nature
Publication Date
Sep 15, 2021
Volume
12
Identifiers
DOI: 10.1038/s41467-021-25550-2
PMID: 34526502
PMCID: PMC8443592
Source
PubMed Central
Keywords
Disciplines
  • Article
License
Unknown

Abstract

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.

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