Referenced in: none

Automatically associated channels: ClC4 , Slo1

Title: Putting the pieces together: a crystal clear window into CLC anion channel regulation.

Authors: Kevin Strange

Journal, date & volume: Channels (Austin), 2011 Mar-Apr , 5, 101-5

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/21317557

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) .