IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v453y2008i7196d10.1038_nature06907.html
   My bibliography  Save this article

The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes

Author

Listed:
  • Austin R. Graves

    (Membrane Transport Biophysics Unit, and,)

  • Patricia K. Curran

    (Membrane Transport Biophysics Unit, and,)

  • Carolyn L. Smith

    (Light Microscopy Facility, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, Building 35, MSC 3701, Bethesda, Maryland 20892, USA)

  • Joseph A. Mindell

    (Membrane Transport Biophysics Unit, and,)

Abstract

Chloride permeation in lysosomes There has been much interest in the CLC family of membrane proteins since it has become apparent that some members are chlorine ion conducting ion channels whilst others are antiporters for chlorine and hydrogen ions. An antiporter is a membrane protein that is involved in active transport of two or more different ligands. In this paper, Graves et al. show that ClC-7 is a Cl−/H+ antiporter in lysosomal membranes, whose activity maintains the correct membrane voltage during acidification of the organelle. Interestingly, this work also reinforces the idea that plasma membrane CLCs are dedicated Cl− channels, whereas 'intracellular' CLCs are antiporters. This represents direct evidence that a CLC protein is responsible for the long-hypothesized chloride permeability of lysosomal membranes.

Suggested Citation

  • Austin R. Graves & Patricia K. Curran & Carolyn L. Smith & Joseph A. Mindell, 2008. "The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes," Nature, Nature, vol. 453(7196), pages 788-792, June.
  • Handle: RePEc:nat:nature:v:453:y:2008:i:7196:d:10.1038_nature06907
    DOI: 10.1038/nature06907
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature06907
    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/nature06907?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. Qiaochu Wang & Zengge Wang & Yizhen Wang & Zhan Qi & Dayong Bai & Chentong Wang & Yuanying Chen & Wenjian Xu & Xili Zhu & Jaepyo Jeon & Jian Xiong & Chanjuan Hao & Michael Xi Zhu & Aihua Wei & Wei Li, 2023. "A gain-of-function TPC2 variant R210C increases affinity to PI(3,5)P2 and causes lysosome acidification and hypopigmentation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. James L. Daly & Chris M. Danson & Philip A. Lewis & Lu Zhao & Sara Riccardo & Lucio Filippo & Davide Cacchiarelli & Daehoon Lee & Stephen J. Cross & Kate J. Heesom & Wen-Cheng Xiong & Andrea Ballabio , 2023. "Multi-omic approach characterises the neuroprotective role of retromer in regulating lysosomal health," Nature Communications, Nature, vol. 14(1), pages 1-19, 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:453:y:2008:i:7196:d:10.1038_nature06907. 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.