Cross-talk between mutant p53 and p62/SQSTM1 augments cancer cell migration by promoting the degradation of cell adhesion proteins

Saptaparna Mukherjee, Martino Maddalena, YiQing Lü, Sebastien Martinez, Nishanth Belugali Nataraj, Ashish Noronha, Sansrity Sinha, Katie Teng, Victoria Cohen-Kaplan, Tamar Ziv, Sharathchandra Arandkar, Ori Hassin, Rishita Chatterjee, Anna-Chiara Pirona, Michal Shreberk-Shaked, Anat Gershoni, Yael Aylon, Zvulun Elazar, Yosef Yarden, Daniel SchramekMoshe Oren*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

Missense mutations in the p53 tumor suppressor abound in human cancer. Common (“hotspot”) mutations endow mutant p53 (mutp53) proteins with oncogenic gain of function (GOF), including enhanced cell migration and invasiveness, favoring cancer progression. GOF is usually attributed to transcriptional effects of mutp53. To elucidate transcription-independent effects of mutp53, we characterized the protein interactome of the p53R273H mutant in cells derived from pancreatic ductal adenocarcinoma (PDAC), where p53R273H is the most frequent p53 mutant. We now report that p53R273H, but not the p53R175H hotspot mutant, interacts with SQSTM1/p62 and promotes cancer cell migration and invasion in a p62-dependent manner. Mechanistically, the p53R273H-p62 axis drives the proteasomal degradation of several cell junction–associated proteins, including the gap junction protein Connexin 43, facilitating scattered cell migration. Concordantly, down-regulation of Connexin 43 augments PDAC cell migration, while its forced overexpression blunts the promigratory effect of the p53R273H-p62 axis. These findings define a mechanism of mutp53 GOF.
Original languageEnglish
Article numbere2119644119
Number of pages12
JournalProceedings of the National Academy of Sciences
Volume119
Issue number17
DOIs
Publication statusPublished - 26 Apr 2022

All Science Journal Classification (ASJC) codes

  • General

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