From glutathione transferase to pore in a CLIC

Brett A. Cromer, Craig J. Morton, Philip G. Board, Michael W. Parker*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    78 Citations (Scopus)

    Abstract

    Many plasma membrane chloride channels have been cloned and characterized in great detail. In contrast, very little is known about intracellular chloride channels. Members of a novel class of such channels, called the CLICs (chloride intracellular channels), have been identified over the last few years. A striking feature of the CLIC family of ion channels is that they can exist in a water-soluble state as well as a membrane-bound state. A major step forward in understanding the functioning of these channels has been the recent crystal structure determination of one family member, CLIC1. The structure confirms that CLICs are members of the glutathione S-transferase superfamily and provides clues as to how CLICs can insert into membranes to form chloride channels.

    Original languageEnglish
    Pages (from-to)356-364
    Number of pages9
    JournalEuropean Biophysics Journal
    Volume31
    Issue number5
    DOIs
    Publication statusPublished - Sept 2002

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