In mitochondria, ATP synthase complexes are arranged in rows of dimers along the edges of the cristae [1][2] [3][4][5]. Dimerisation depends on the e-subunit and possibly other supernumerary subunits [6][7][8][9][5]. It has been proposed that the mitochondrial permeability transition pore is associated with dimers of ATP synthase [10].


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  2. Dudkina NV, Heinemeyer J, Keegstra W, Boekema EJ & Braun H-P (2005) Structure of dimeric ATP synthase from mitochondria: an angular association of monomers induces the strong curvature of the inner membrane. FEBS Lett 579, 5769-72
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  7. Arselin G, Giraud M-F, Dautant A, Vaillier J, Brèthes D, Coulary-Salin B, Schaeffer J & Velours J (2003) The GxxxG motif of the transmembrane domain of subunit e is involved in the dimerization/oligomerization of the yeast ATP synthase complex in the mitochondrial membrane. Eur J Biochem 270, 1875-84
  8. Bustos DM & Velours J (2005) The modification of the conserved GXXXG motif of the membrane-spanning segment of subunit g destabilizes the supramolecular species of yeast ATP synthase. J Biol Chem 280, 29004-10
  9. Paumard P, Arselin G, Vaillier J, Chaignepain S, Bathany K, Schmitter JMarie, Brèthes D & Velours J (2002) Two ATP synthases can be linked through subunits i in the inner mitochondrial membrane of Saccharomyces cerevisiae. Biochemistry 41, 10390-6
  10. Giorgio V, von Stockum S, Antoniel M, Fabbro A, Fogolari F, Forte M, Glick GD, Petronilli V, Zoratti M, Szabó I, Lippe G & Bernardi P (2013) Dimers of mitochondrial ATP synthase form the permeability transition pore. Proc Natl Acad Sci U S A 110, 5887-92