Bcl-xL forms an ion channel in synthetic lipid membranes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-01

AUTHORS

A J Minn, P Vélez, S L Schendel, H Liang, S W Muchmore, S W Fesik, M Fill, C B Thompson

ABSTRACT

Bcl-2-related proteins are critical regulators of cell survival that are localized to the outer mitochondrial, outer nuclear and endoplasmic reticulum membranes. 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 toxins. A key feature of these pore-forming domains is the ability to form ion channels in biological membranes. 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. More... »

PAGES

353-357

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/385353a0

DOI

http://dx.doi.org/10.1038/385353a0

DIMENSIONS

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PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9002522


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