Journal of Biological Chemistry · 1996 · 247 citations · 24 references
Life SciencesBiochemistryBiophysicsBioenergeticsIntracellular TransportMitochondrial BiologyIon Channel PhysiologyIon Channel RegulationIon ChannelsMitochondrial MembranesMitochondrial PhysiologyMitochondrial TransportChannelsMitochondrial Ion TransportMitochondrial Membrane Transport ChannelsPorin FunctionPorin ProteinsVoltage-dependent Ion ChannelsVoltage-gated ChannelsVoltage-gated Ion Channels
A voltage-gated channel, called VDAC (mitochondrial porin) is known to be responsible for most of the metabolite flux across the mitochondrial outer membrane. Here, direct measurements of ATP flux through VDAC channels reconstituted into planar phospholipid membranes establish that VDAC is sufficient to provide passage for ATP efflux from mitochondria. Further, the gating of the channel can shut down ATP flux completely while, simultaneously, allowing the flow of small ions. Thus, these channels are ideally suited to control ATP flux through the mitochondrial outer membrane and, consequently, mitochondrial function. The block to ATP flow through the closed state is likely to be not steric but electrostatic. A voltage-gated channel, called VDAC (mitochondrial porin) is known to be responsible for most of the metabolite flux across the mitochondrial outer membrane. Here, direct measurements of ATP flux through VDAC channels reconstituted into planar phospholipid membranes establish that VDAC is sufficient to provide passage for ATP efflux from mitochondria. Further, the gating of the channel can shut down ATP flux completely while, simultaneously, allowing the flow of small ions. Thus, these channels are ideally suited to control ATP flux through the mitochondrial outer membrane and, consequently, mitochondrial function. The block to ATP flow through the closed state is likely to be not steric but electrostatic.
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Decoding of cytosolic calcium oscillations in the mitochondria
György Hajnóczky, Lawrence D. Gaspers, M B Seitz et al. · Cell · 1995 · 1.1K citations · Full text
ATP-sensitive K+ channel in the mitochondrial inner membrane
I Inoue, Hideki Nagase, Tomihiko Higuti · Nature · 1991 · 753 citations
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