The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Channel formation by antiapoptotic protein Bcl-2
Open accessAbstract
Bcl-2 is the prototypical member of a large family of apoptosis-regulating proteins, consisting of blockers and promoters of cell death. The three-dimensional structure of a Bcl-2 homologue, Bcl-X L , suggests striking similarity to the pore-forming domains of diphtheria toxin and the bacterial colicins, prompting exploration of whether Bcl-2 is capable of forming pores in lipid membranes. Using chloride efflux from KCl-loaded unilamellar lipid vesicles as an assay, purified recombinant Bcl-2 protein exhibited pore-forming activity with properties similar to those of the bacterial toxins, diphtheria toxin, and colicins, i.e., dependence on low pH and acidic lipid membranes. In contrast, a mutant of Bcl-2 lacking the two core hydrophobic α-helices (helices 5 and 6), predicted to be required for membrane insertion and channel formation, produced only nonspecific effects. In planar lipid bilayers, where detection of single channels is possible, Bcl-2 formed discrete ion-conducting, cation-selective channels, whereas the Bcl-2 (Δh5, 6) mutant did not. The most frequent conductance observed (18 ± 2 pS in 0.5 M KCl at pH 7.4) is consistent with a four-helix bundle structure arising from Bcl-2 dimers. However, larger channel conductances (41 ± 2 pS and 90 ± 10 pS) also were detected with progressively lower occurrence, implying the step-wise formation of larger oligomers of Bcl-2 in membranes. These findings thus provide biophysical evidence that Bcl-2 forms channels in lipid membranes, suggesting a novel function for this antiapoptotic protein.
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Cites
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Molecular biology of Bax and Bak activation and action
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Metadata
- Authors
- Schendel, S. L., Xie, Z., Montal, M. O., Matsuyama, S., Montal, M., & Reed, J. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-05-13
- Volume
- 94
- Issue
- 10
- Pages
- 5113-5118
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2032221839
- Cited by
- 602
- References
- 1
- FWCI
- 31.39
- Type
- journal article
- Language
- en
- Open access
- green
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