The C terminus of Bax inhibitor-1 forms a Ca2+-permeable channel pore.

@article{Bultynck2012TheCT,
  title={The C terminus of Bax inhibitor-1 forms a Ca2+-permeable channel pore.},
  author={Geert Bultynck and Santeri Kiviluoto and Nadine Henke and Hristina Ivanova and Lars Schneider and Volodymyr Rybalchenko and Tomas Luyten and Koen Nuyts and Wim M De Borggraeve and Ilya B Bezprozvanny and Jan B Parys and Humbert de Smedt and Ludwig Missiaen and Axel Methner},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 4},
  pages={2544-57}
}
Bax inhibitor-1 (BI-1) is a multitransmembrane domain-spanning endoplasmic reticulum (ER)-located protein that is evolutionarily conserved and protects against apoptosis and ER stress. Furthermore, BI-1 is proposed to modulate ER Ca(2+) homeostasis by acting as a Ca(2+)-leak channel. Based on experimental determination of the BI-1 topology, we propose that its C terminus forms a Ca(2+) pore responsible for its Ca(2+)-leak properties. We utilized a set of C-terminal peptides to screen for Ca(2… CONTINUE READING
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