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Walerych, Dawid; Lisek, Kamil; Sommaggio, Roberta; Piazza, Silvano; Ciani, Yari; Dalla, Emiliano; Rajkowska, Katarzyna; Gaweda-Walerych, Katarzyna; Ingallina, Eleonora; Tonelli, Claudia; Morelli, Marco J; Amato, Angela; Eterno, Vincenzo; Zambelli, Alberto; Rosato, Antonio; Amati, Bruno; Wiśniewski, Jacek R; Del Sal, Giannino
Nature cell biology, 08/2016, Letnik: 18, Številka: 8Journal Article
In cancer, the tumour suppressor gene TP53 undergoes frequent missense mutations that endow mutant p53 proteins with oncogenic properties. Until now, a universal mutant p53 gain-of-function program has not been defined. By means of multi-omics: proteome, DNA interactome (chromatin immunoprecipitation followed by sequencing) and transcriptome (RNA sequencing/microarray) analyses, we identified the proteasome machinery as a common target of p53 missense mutants. The mutant p53-proteasome axis globally affects protein homeostasis, inhibiting multiple tumour-suppressive pathways, including the anti-oncogenic KSRP-microRNA pathway. In cancer cells, p53 missense mutants cooperate with Nrf2 (NFE2L2) to activate proteasome gene transcription, resulting in resistance to the proteasome inhibitor carfilzomib. Combining the mutant p53-inactivating agent APR-246 (PRIMA-1MET) with the proteasome inhibitor carfilzomib is effective in overcoming chemoresistance in triple-negative breast cancer cells, creating a therapeutic opportunity for treatment of solid tumours and metastasis with mutant p53.
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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in: SICRIS
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