2013
DOI: 10.1016/j.biocel.2012.05.017
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ATP synthase oligomerization: From the enzyme models to the mitochondrial morphology

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Cited by 75 publications
(70 citation statements)
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“…Moreover, deletion of subunit e and g of ATP synthase F1 in yeast leads to no dimerization and oligomerization where the classical cristae shape did not exist; this was replaced by onion-shape mitochondria, although the enzyme activity is fully functional. These data support the idea of the correlation between the organization of ATP synthase and mitochondrial morphology (Habersetzer et al 2013). Two previous publications suggested that ATP5B might be involved in mitochondrial dynamics.…”
Section: Introductionsupporting
confidence: 90%
See 1 more Smart Citation
“…Moreover, deletion of subunit e and g of ATP synthase F1 in yeast leads to no dimerization and oligomerization where the classical cristae shape did not exist; this was replaced by onion-shape mitochondria, although the enzyme activity is fully functional. These data support the idea of the correlation between the organization of ATP synthase and mitochondrial morphology (Habersetzer et al 2013). Two previous publications suggested that ATP5B might be involved in mitochondrial dynamics.…”
Section: Introductionsupporting
confidence: 90%
“…The ATP synthase complex is constituted by F 1 part (subunits a, b, g, d, and 1) and F parts (subunits b, F6, d, f, a, A6L, and OSCP), and uses the electrochemical proton gradient produced by the electron transport chain complexes, to synthesize ATP (Habersetzer et al 2013).…”
Section: Introductionmentioning
confidence: 99%
“…Moreover, using digitonin extraction, hr CN PAGE, in-gel ATPase activity staining and native immunoblotting, we show that ecto-F 0 F 1 complexes have a similar molecular mass to the mitochondrial ATP synthase monomers and preserve their sensitivity to the inhibitor oligomycin. Detection of only monomers in PM may be a consequence of the low concentration of ecto-F 0 F 1 complexes unable to form polymers, but it is consistent with the uniquely mitochondrial role of ATP synthase dimers to help formation of cristae (Habersetzer et al 2013), which are absent in lipid rafts (Gorai et al 2012).…”
Section: Discussionmentioning
confidence: 81%
“…One of the possibilities of MA-5 acting mechanisms is the effect on the oligomerization of ATP synthase. The oligomerization of ATP synthase is essential for the maintenance of cristae junctions (Habersetzer et al 2013). In addition, the oligomerization of ATP synthase does increase the local pH gradient and membrane potential and optimizes ATP synthesis without changing whole mitochondrial membrane potential (Strauss et al 2008).…”
Section: Discussionmentioning
confidence: 99%