Regulation of Bnip3 death pathways by calcium, phosphorylation, and hypoxia-reoxygenation.

  title={Regulation of Bnip3 death pathways by calcium, phosphorylation, and hypoxia-reoxygenation.},
  author={Regina M Graham and John W Thompson and Jianqin Wei and Nanette Hahr Bishopric and Keith A. Webster},
  journal={Antioxidants & redox signaling},
  volume={9 9},
Bnip3 is a proapoptotic member of the Bcl-2 family of death-regulating proteins that promote the intrinsic pathway of programmed cell death. The Bnip3 death program requires membrane insertion through an N-terminal transmembrane domain that directs the protein to mitochondrial and endoplasmic reticular (ER) membranes. We have reported that simulated ischemia induces transcription of the Bnip3 gene, and Bnip3 protein is stabilized by acidosis. Bnip3 programmed death is atypical, with features of… CONTINUE READING
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