Jul 26, 2011 · In this study, we showed that p53 suppressed BNIP3 expression by directly binding to the p53-response element motif and recruiting corepressor mSin3a to the BNIP3 promoter. The DNA-binding site of p53 must remain intact for the protein to suppress the BNIP3 promoter.

May 6, 2013 · Loss of Bnip3 function completely abrogated autophagy and cell death induced by p53. Hence, our findings reveal a novel signaling axis between mitochondrial localization of p53 and Bnip3 for autophagy and cell death that may explain more fundamentally how p53 dually regulates autophagy and cell death of ventricular myocytes during cardiac stress.

Jan 21, 2019 · Our results showed that wild-type p53 in radioresistant cancers overcomes chronic radiation exposure through p53/BNIP3-dependent mitophagy and limited glycolytic remodeling.

Aug 8, 2011 · In this study, we showed that p53 suppressed BNIP3 expression by directly binding to the p53-response element motif and recruiting corepressor mSin3a to the BNIP3 promoter. The DNA-binding site of p53 must remain intact for the protein to suppress the BNIP3 promoter.

Isogenic p53-null radioresistant cancer cells established through cumulative irradiation showed decreased oxygen consumption and increased glycolysis with compromised mitochondria, corresponding with their enhanced sensitivity to drugs that target glycolysis.

May 6, 2013 · However, whether p53 regulates Bnip3 and autophagy is unknown. Herein, we provide new compelling evidence for a novel signaling axis that commonly links p53 and Bnip3 for autophagy and cell death. p53 overexpression increased endogenous Bnip3 mRNA and protein levels resulting in mitochondrial defects leading to loss of mitochondrial ΔΨ m .

Abstract—Myocardial ischemia and angiotensin II activate the tumor suppressor p53 protein, which promotes cell death. Previously, we showed that the Bcl-2 death gene Bnip3 is highly induced during ischemia, where it triggers mitochondrial perturbations resulting …

Herein, we provide new compelling evidence for a novel signaling axis that commonly links p53 and Bnip3 for autophagy and cell death. p53 overexpression increased endogenous Bnip3 mRNA and protein levels resulting in mitochondrial defects leading to loss of mitochondrial ΔΨ(m).

Our results suggest that Bnip3L can suppress tumor xenograft growth in vivo and is a mediator of p53-dependent apoptosis under hypoxia. The regulation of Bnip3L by p53 provides a novel mechanism by which p53 acts as a tumor suppressor in vivo.

In vivo, Bnip3L knockdown promotes tumorigenicity of wild-type versus mutant p53-expressing tumors. Thus, Bnip3L, capable of attenuating tumorigenicity, mediates p53-dependent apoptosis under hypoxia, which provides a novel understanding of p53 in tumor suppression.