Format

Send to

Choose Destination
Sci Signal. 2014 Sep 16;7(343):pe22. doi: 10.1126/scisignal.2005764.

Bax inhibitor-1 is likely a pH-sensitive calcium leak channel, not a H+/Ca2+ exchanger.

Author information

1
KU Leuven, Laboratory of Molecular and Cellular Signaling, Department of Cellular and Molecular Medicine, Leuven, Belgium. geert.bultynck@med.kuleuven.be axel.methner@gmail.com.
2
KU Leuven, Laboratory of Molecular and Cellular Signaling, Department of Cellular and Molecular Medicine, Leuven, Belgium.
3
Focus Program Translational Neuroscience (FTN), Rhine Main Neuroscience Network (rmn), Johannes Gutenberg University Medical Center Mainz, Department of Neurology, Mainz, Germany. geert.bultynck@med.kuleuven.be axel.methner@gmail.com.

Abstract

The endoplasmic reticulum (ER) plays a key role in the synthesis, folding, and sorting of proteins, and disturbances of this delicate system can cause cell death. The ER also serves as the major intracellular calcium (Ca(2+)) store, and release of Ca(2+) from this store controls diverse cellular functions. At the interface of both these functions of the ER is Bax inhibitor-1 (BI-1), an evolutionarily conserved multifunctional protein that mediates Ca(2+) efflux from the ER and protects against ER stress. Several mechanisms have been proposed to explain how BI-1 might mediate Ca(2+) efflux from the ER. Chang et al. present structural evidence that a bacterial homolog of BI-1, BsYetJ, is a pH-sensitive Ca(2+) leak channel. This finding not only sheds a new light on ER Ca(2+) efflux mediated by BI-1, but also provides a tentative function for other members of the BI-1 protein family.

PMID:
25227609
DOI:
10.1126/scisignal.2005764
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center