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Design, function and structure of a monomeric ClC transporter

Author

Listed:
  • 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)

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?

Suggested Citation

  • Janice L. Robertson & Ludmila Kolmakova-Partensky & Christopher Miller, 2010. "Design, function and structure of a monomeric ClC transporter," Nature, Nature, vol. 468(7325), pages 844-847, December.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7325:d:10.1038_nature09556
    DOI: 10.1038/nature09556
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    Cited by:

    1. Keri A McKiernan & Anna K Koster & Merritt Maduke & Vijay S Pande, 2020. "Dynamical model of the CLC-2 ion channel reveals conformational changes associated with selectivity-filter gating," PLOS Computational Biology, Public Library of Science, vol. 16(3), pages 1-24, March.
    2. Mingfeng Zhang & Yuanyue Shan & Charles D. Cox & Duanqing Pei, 2023. "A mechanical-coupling mechanism in OSCA/TMEM63 channel mechanosensitivity," Nature Communications, Nature, vol. 14(1), pages 1-9, December.

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