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- W2047841896 abstract "Programmed cell death, or apoptosis is an essential biological process in embryogenesis or in the maintenance of homeostasis in higher eukaryotes. In the mitochondrial apoptotic pathways, the pro-apoptotic Bcl-2 family proteins BAK and BAX, upon activation by death signals, are believed to form large oligomeric pores via homodimer formation in the mitochondrial outer membrane. Through these pores of an unknown structure, many apoptotic factors are released from the intermembrane space into the cytoplasm, where they initiate the cascade of events that lead to cell death. We have determined the topographic locations of the residues in the helices α4, α5 and α6 of BAK in the BAK oligomeric pore using the site-directed spin labeling method and/or the IASD (4-acetamido-4′-((iodoacetyl)amino)stilbene-2,2′disulfonic acid) labeling approach. Accessibility parameters of oxygen and NiEDDA to residues in helix α5 showed that the helix is exposed to the membrane on one side, with the opposite side in tertiary contact. The IASD labeling pattern in helix α5 also revealed the same. These results were consistent with the predictions by the BAX ‘BH3-in-groove homodimer’, a recently reported X-ray crystallographic structure of a dimer of a truncated BAX consisting of helices α2-α5. The membrane immersion-depths of selected residues in helices α4 and α5 indicated that the adsorption of the BAK ‘BH3-in-groove homodimer' to the membrane surface is mediated by the hydrophobic surface of the homodimer. The helix α6 was also adsorbed to the membrane surface, with its N-terminus deeper than the C-terminus. In summary, the data suggest that BAK proteins form a lipidic pore, unlike the channel forming domains of certain bacterial toxins such as diphtheria toxin or colicin molecules. The results provide further insights into the mechanism of formation of the mitochondrial apoptotic pores by BAX or BAK." @default.
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- W2047841896 date "2014-01-01" @default.
- W2047841896 modified "2023-09-28" @default.
- W2047841896 title "Interaction of the BAK Homodimer with the Membrane" @default.
- W2047841896 doi "https://doi.org/10.1016/j.bpj.2013.11.208" @default.
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