IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v427y2004i6977d10.1038_nature02314.html
   My bibliography  Save this article

Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels

Author

Listed:
  • Alessio Accardi

    (Brandeis University)

  • Christopher Miller

    (Brandeis University)

Abstract

ClC Cl- channels make up a large molecular family, ubiquitous with respect to both organisms and cell types. In eukaryotes, these channels fulfill numerous biological roles requiring gated anion conductance, from regulating skeletal muscle excitability to facilitating endosomal acidification by (H+)ATPases. In prokaryotes, ClC functions are unknown except in Escherichia coli, where the ClC-ec1 protein promotes H+ extrusion activated in the extreme acid-resistance response common to enteric bacteria. Recently, the high-resolution structure of ClC-ec1 was solved by X-ray crystallography. This primal prokaryotic ClC structure has productively guided understanding of gating and anion permeation in the extensively studied eukaryotic ClC channels. We now show that this bacterial homologue is not an ion channel, but rather a H+-Cl- exchange transporter. As the same molecular architecture can support two fundamentally different transport mechanisms, it seems that the structural boundary separating channels and transporters is not as clear cut as generally thought.

Suggested Citation

  • Alessio Accardi & Christopher Miller, 2004. "Secondary active transport mediated by a prokaryotic homologue of ClC Cl- channels," Nature, Nature, vol. 427(6977), pages 803-807, February.
  • Handle: RePEc:nat:nature:v:427:y:2004:i:6977:d:10.1038_nature02314
    DOI: 10.1038/nature02314
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature02314
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature02314?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Zhao Yang & Xue Zhang & Shiwei Ye & Jingtao Zheng & Xiaowei Huang & Fang Yu & Zhenguo Chen & Shiqing Cai & Peng Zhang, 2023. "Molecular mechanism underlying regulation of Arabidopsis CLCa transporter by nucleotides and phospholipids," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Yangzhuoqun Wan & Shuangshuang Guo & Wenxuan Zhen & Lizhen Xu & Xiaoying Chen & Fangyue Liu & Yi Shen & Shuangshuang Liu & Lidan Hu & Xinyan Wang & Fengcan Ye & Qinrui Wang & Han Wen & Fan Yang, 2024. "Structural basis of adenine nucleotides regulation and neurodegenerative pathology in ClC-3 exchanger," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Lilia Leisle & Kin Lam & Sepehr Dehghani-Ghahnaviyeh & Eva Fortea & Jason D. Galpin & Christopher A. Ahern & Emad Tajkhorshid & Alessio Accardi, 2022. "Backbone amides are determinants of Cl− selectivity in CLC ion channels," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:427:y:2004:i:6977:d:10.1038_nature02314. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.