Putting the pieces together: A crystal clear window into CLC anion channel regulation

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Abstract

CLC anion transport proteins function as Cl (-) channels and Cl (-) /H (+) exchangers and are found in all major groups of life including archaebacteria. Early electrophysiological studies suggested that CLC anion channels have two pores that are opened and closed independently by a "fast" gating process operating on a millisecond timescale, and a "common" or "slow" gate that opens and closes both pores simultaneously with a timescale of seconds (Figure 1A). Subsequent biochemical and molecular experiments suggested that CLC channels/transporters are homodomeric proteins ( 1-3) .

Original languageEnglish
Pages (from-to)101-105
Number of pages5
JournalChannels
Volume5
Issue number2
DOIs
Publication statusPublished - Mar 2011
Externally publishedYes

Keywords

  • ATP binding
  • C. Elegans
  • Channel regulation
  • Cystathionine-β-synthetase domain
  • Phosphorylation
  • Ste20 kinase
  • X-ray crystallography

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