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Large transient capacitive currents in wild-type lysosomal Cl−/H+ antiporter ClC-7 and residual transport activity in the proton glutamate mutant E312A
Pusch and Zifarelli show that the lysosomal 2 Cl−/1 H+ antiporter ClC-7 mediates large, transient capacitive currents, which depend on external pH and internal Cl−. Unlike in other mammalian CLC antiporters, mutation of a conserved proton glutamate residue in ClC-7 does not abolish transport currents.
