Are chloride intracellular ion channel proteins (CLICs) really channels?
L.J. Brown1, D.R. Littler2, A. Mynott2, S.J. Harrop2, S.N. Breit3, M. Mazzanti4 and P.M.G. Curmi2, 1Department of Chemistry and Biomolecular Sciences, Macquarie University, NSW 2109, Australia, 2School of Physics, University of New South Wales, NSW 2052, Australia, 3Centre for Immunology, St Vincent’s Hospital, Sydney NSW 2010, and 4University or Rome, La Sapienza, Roma, Italy. Most proteins adopt a well-defined three-dimensional structure, however, it is increasingly recognized that some proteins can exist with at least two or more stable conformations. Recently, a class of Chloride Intracellular ion Channel proteins (CLICs) has been shown to exist in both soluble and integral membrane forms. Members of this class of ion channels have a CLIC domain of approximately 240 amino acids in length and vary widely in their cellular and sub-cellular distribution. They are associated with a variety of intracellular membranes and are involved in numerous diverse physiological processes including
