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• W2186543992 abstract "Ca(2+) transfer from the endoplasmic reticulum (ER) to the mitochondria critically controls cell survival and cell death decisions. Different oncogenes and deregulation of tumor suppressors exploit this mechanism to favor the survival of altered, malignant cells. Two recent studies of the Pinton team revealed a novel, non-transcriptional function of cytosolic p53 in cell death. During cell stress, p53 is recruited to the ER and the ER-mitochondrial contact sites. This results in augmented ER Ca(2+) levels by enhancing sarco/endoplasmic reticulum Ca(2+) ATPase (SERCA) activity, ultimately promoting mitochondrial Ca(2+) overload. The boosting of toxic Ca(2+) signaling by p53 appears to be a critical component of the cell death-inducing properties of chemotherapeutic agents and anti-cancer treatments, like photodynamic stress. Strikingly, the resistance of p53-deficient cancer cells to these treatments could be overcome by facilitating Ca(2+) transfer between the ER and the mitochondria via overexpression of SERCA or of the mitochondrial Ca(2+) uniporter (MCU). Importantly, these concepts have also been supported by in vivo Ca(2+) measurements in tumor masses in mice. Collectively, these studies link for the first time the major tumor suppressor, p53, to Ca(2+) signaling in dictating cell-death outcomes and by the success of anti-cancer treatments." @default.
• W2186543992 created "2016-06-24" @default.
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• W2186543992 date "2015-03-07" @default.
• W2186543992 modified "2023-09-23" @default.
• W2186543992 title "p53 and Ca2+ signaling from the endoplasmic reticulum: partners in anti-cancer therapies" @default.
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• W2186543992 doi "https://doi.org/10.18632/oncoscience.139" @default.
• W2186543992 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4394128" @default.
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