Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase
| العنوان: | Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase |
|---|---|
| المؤلفون: | Panah Nabili, Benjamin J. Flaherty, Ying Bei Chen, Kambiz N. Alavian, Gordon C. Shore, Hongmei Li, Laura Bonanni, Lu Zeng, Emma Lazrove, Shanta M. Messerli, Elizabeth A. Jonas, Morven Graham, Christopher Rahner, Peter K. Smith, Ewan C. McNay, Maria A. Mariggiò, Leon P. Collis, Silvio Sacchetti, J. Marie Hardwick |
| المصدر: | BASE-Bielefeld Academic Search Engine Nature cell biology |
| مصطلحات موضوعية: | Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone, Patch-Clamp Techniques, Time Factors, ATPase, Recombinant Fusion Proteins, bcl-X Protein, Biology, Mitochondrion, Transfection, Hippocampus, Article, Piperazines, Nitrophenols, chemistry.chemical_compound, Adenosine Triphosphate, Oxygen Consumption, Animals, Enzyme Inhibitors, Cells, Cultured, bcl-2-Associated X Protein, Membrane potential, Membrane Potential, Mitochondrial, Neurons, Sulfonamides, ATP synthase, Hydrolysis, ATPase complex, Biphenyl Compounds, Cell Biology, Mitochondrial Proton-Translocating ATPases, Molecular biology, Cell biology, Mitochondria, Rats, bcl-2 Homologous Antagonist-Killer Protein, chemistry, Mitochondrial Membranes, Synapses, biology.protein, Proton Ionophores, Carbonyl cyanide-p-trifluoromethoxyphenylhydrazone, Oligomycins, RNA Interference, Energy Metabolism, Adenosine triphosphate, Bcl-2 Homologous Antagonist-Killer Protein |
| الوصف: | Anti-apoptotic Bcl2 family proteins such as Bcl-x(L) protect cells from death by sequestering apoptotic molecules, but also contribute to normal neuronal function. We find in hippocampal neurons that Bcl-x(L) enhances the efficiency of energy metabolism. Our evidence indicates that Bcl-x(L)interacts directly with the β-subunit of the F(1)F(O) ATP synthase, decreasing an ion leak within the F(1)F(O) ATPase complex and thereby increasing net transport of H(+) by F(1)F(O) during F(1)F(O) ATPase activity. By patch clamping submitochondrial vesicles enriched in F(1)F(O) ATP synthase complexes, we find that, in the presence of ATP, pharmacological or genetic inhibition of Bcl-x(L) activity increases the membrane leak conductance. In addition, recombinant Bcl-x(L) protein directly increases the level of ATPase activity of purified synthase complexes, and inhibition of endogenous Bcl-x(L) decreases the level of F(1)F(O) enzymatic activity. Our findings indicate that increased mitochondrial efficiency contributes to the enhanced synaptic efficacy found in Bcl-x(L)-expressing neurons. |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::738000635026466cf789021accdc27bfTest http://hdl.handle.net/11564/223205Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....738000635026466cf789021accdc27bf |
| قاعدة البيانات: | OpenAIRE |
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