The chloride intracellular ion channel (CLIC) protein family is highly conserved in vertebrates. These family members are unique, showing as both monomeric soluble proteins and integral membrane proteins which act as chloride selective ion channels. Structural studies have indicated that CLIC proteins with soluble forms adopt a glutathione S-transferase (GST) fold, and hence they are distributed to the GST fold protein family. Currently, the evidence exhibits that CLIC has glutaredoxin-like glutathione-dependent oxidoreductase enzymatic activity. CLIC has been demonstrated typical glutaredoxin-like activity by using 2-hydroxyethyl disulfide as a substrate. Mutagenesis assays validated cysteine 24 as the catalytic cysteine residue in CLIC1 that is consistent with its identified structure. CLIC1 was testified to decrease dehydroascorbate and sodium selenite in a glutathione-dependent manner. Previous electrophysiological experiments found that the drugs IAA-94 and A9C can specifically block the CLIC channel activity. Furthermore, the same compounds inhibit the activity of CLIC1 oxidoreductase. It is the first time to assign a functional activity for the soluble form of CLIC proteins.
CLIC family members are highly conserved in vertebrates and this family comprises six evolutionarily conserved proteins in humans, CLIC1 to CLIC6. CLIC proteins exist as globular soluble and/or as integral membrane proteins. These proteins are known to spontaneously transit from their soluble state into integral membrane form, working as an anion-selective channel. CLIC1 channel conductance is regulated by several factors including redox, cholesterol, pH, and membrane phospholipid composition. Here show the part of CLIC members in humans.
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