Bcl-xL forms an ion channel in synthetic lipid membranes

Andy J. Minn, Patricio Vélez, Sharon L. Schendel, Heng Liang, Steven W. Muchmore, Stephen W. Fesik, Michael Fill and Craig B. Thompson
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Andy J. Minn: The University of Chicago
Patricio Vélez: Loyola University of Chicago Stritch School of Medicine
Sharon L. Schendel: Purdue University
Heng Liang: NMR Resarch, Abbott Laboratories
Steven W. Muchmore: Abbott Laboratories
Stephen W. Fesik: NMR Resarch, Abbott Laboratories
Michael Fill: Loyola University of Chicago Stritch School of Medicine
Craig B. Thompson: The University of Chicago

Nature, 1997, vol. 385, issue 6614, 353-357

Abstract: Abstract Bcl-2-related proteins are critical regulators of cell survival that are localized to the outer mitochondrial, outer nuclear and endoplasmic reticulum membranes1–4. Despite their physiological importance, the biochemical function of Bcl-2-related proteins has remained elusive. The three-dimensional structure of Bcl-xL, an inhibitor of apoptosis, was recently shown to be similar to the structures of the pore-forming domains of bacterial toxins5. A key feature of these pore-forming domains is the ability to form ion channels in biological membranes6,7. Here we demonstrate that Bcl-xL shares this functional feature. Like the bacterial toxins, Bcl-xL can insert into either synthetic lipid vesicles or planar lipid bilayers and form an ion-conducting channel. This channel is pH-sensitive and becomes cation-selective at physiological pH. The ion-conducting channel(s) formed by Bcl-xL display multiple conductance states that have identical ion selectivity. Together, these data suggest that Bcl-xL may maintain cell survival by regulating the permeability of the intracellular membranes to which it is distributed.

Date: 1997
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DOI: 10.1038/385353a0

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