Patch-clamping of the inner mitochondrial membrane reveals a voltage-dependent ion channel.
The prime function of mitochondria is to provide the cell with adenosine triphosphate (ATP). ATP synthesis is driven by the protonmotive force (delta p), which is generated and maintained across the inner mitochondrial membrane (IMM) by the activity of the respiratory chain. It is widely believed that the IMM is unlikely to contain ion channels like those present in the plasma membrane, because the high rates of ion transport characteristic of open channels would be expected to dissipate the delta p. Although the small size of the organelle has prevented the use of classical electrophysiological methods, the recent introduction of the patch-clamp technique, which allows currents to be recorded from very small cells, has enabled us to test this hypothesis. By patch-clamping the IMM, we have identified a slightly anion-selective channel, which is voltage-dependent and has a mean conductance of 107 pS in the presence of symmetrical 150 mM KCl.
D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000818:Animals; D000838:Anions; D002463:Cell Membrane Permeability; D002712:Chlorides / Q000378:metabolism; D004553:Electric Conductivity; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000502:physiology*; D007473:Ion Channels / Q000502:physiology*; D008564:Membrane Potentials; D051379:Mice; D008839:Microelectrodes; D008854:Microscopy, Electron; D008928:Mitochondria / Q000648:ultrastructure*; D011188:Potassium / Q000378:metabolism
D000838:Anions; D002712:Chlorides; D007473:Ion Channels; D000255:Adenosine Triphosphate; D011188:Potassium