Estévez, R., Schroeder, B. C., Accardi, A., Jentsch, T. J. & Pusch, M. Conservation of chloride channel structure revealed by an inhibitor binding site in ClC-1.
Mankodi, A. et al. Expanded CUG repeats trigger aberrant splicing of ClC-1 chloride channel pre-mRNA and hyperexcitability of skeletal muscle in myotonic dystrophy.
Saviane, C., Conti, F. & Pusch, M. The muscle chloride channel ClC-1 has a double-barreled appearance that is differentially affected in dominant and recessive myotonia.
This compound, 4,4'-octanamidostilbene-2,2′-disulfonate (OADS), inhibits ClC-ec1 with low micromolar affinity and has no specific effect on a CLC channel (ClC-1).
Since voltage-dependent gating is strictly coupled to ion permeation in ClC-1 channels, the changed pore properties result in different fast and slow gating.
We utilized the Caenorhabditis elegans CLC-1/2/Ka/Kb anion channel homolog CLH-3b to characterize the regulatory roles of CLC cytoplasmic domains.
clc-1 is predicted to function in epithelial cohesion.
Thus, increased CLC-1 in response to infection could strengthen the epithelial layers to resist pathogenesis.
Two genes, lys-1 and clc-1, were required for normal resistance to S. aureus.
clc-1 encodes a claudin-like protein, and its expression has been seen to be induced upon infection [39], [59].
