title: Putting the pieces together: a crystal clear window into CLC anion channel regulation.
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) .
authors.affiliation: Boylan Center for Cellular and Molecular Physiology, Mount Desert Island Biological Laboratory; Salisbury Cove, ME, USA. kstrange@mdibl.org
authors.forename: Kevin
authors.initials: K
authors.lastname: Strange
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D000090007:CLC-2 Chloride Channels; D017173:Caenorhabditis elegans; D018118:Chloride Channels / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods; D003541:Cystathionine beta-Synthase / Q000737:chemistry; D008024:Ligands; D008564:Membrane Potentials; D008968:Molecular Conformation; D016296:Mutagenesis; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: C086321:CLC-1 channel; D000090007:CLC-2 Chloride Channels; C097503:CLC-5 chloride channel; D018118:Chloride Channels; D008024:Ligands; D000255:Adenosine Triphosphate; D003541:Cystathionine beta-Synthase