Design, function and structure of a monomeric ClC transporter

Janice L. Robertson, Ludmila Kolmakova-Partensky and Christopher Miller ()
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Janice L. Robertson: Howard Hughes Medical Institute, Brandeis University
Ludmila Kolmakova-Partensky: Howard Hughes Medical Institute, Brandeis University
Christopher Miller: Howard Hughes Medical Institute, Brandeis University

Nature, 2010, vol. 468, issue 7325, 844-847

Abstract: Why use two when one will do? Channels and transporters of the ClC family are homodimeric, but the aqueous pores for anion diffusion in the channels and the ion-coupling chambers that coordinate Cl− and H+ antiport in the transporters are contained wholly within each subunit of the homodimer. This suggests that these complexes function as 'parallel pathways', a supposition that is confirmed in an experiment in which mutations were used to destabilize the dimer interface of a ClC Cl−/H+ exchanger from Escherichia coli. The resulting mutant channel is monomeric, yet is functionally nearly identical to the wild-type channel. This means that cross-subunit interaction is not required for Cl−/H+ exchange in ClC transporters, which prompts the question: why is the wild-type transporter a homodimer?

Date: 2010
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DOI: 10.1038/nature09556

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