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).
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