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1 Department of Neurobiology, Pharmacology, and Physiology, The University of Chicago, Chicago, IL 60637, USA2 Department of Molecular and Cellular Physiology, University of Cincinnati, Cincinnati, OH 45267, USA3 Department of Pediatrics, University of Iowa, Iowa City, IA 52242, Chicago, IL 60637, USA
CLC-3, a member of the CLC family of chloride channels, mediates function in many cell types in the body. The multifunctional calcium–calmodulin-dependent protein kinase II (CaMKII) has been shown to activate recombinant CLC-3 stably expressed in tsA cells, a human embryonic kidney cell line derivative, and natively expressed channel protein in a human colonic tumour cell line T84. We examined the CaMKII-dependent regulation of CLC-3 in a smooth muscle cell model as well as in the human colonic tumour cell line, HT29, using whole-cell voltage clamp. In CLC-3-expressing cells, we observed the activation of a Cl– conductance following intracellular introduction of the isolated autonomous CaMKII into the voltage-clamped cell via the patch pipette. The CaMKII-dependent Cl– conductance was not observed following exposure of the cells to 1 µM autocamtide inhibitory peptide (AIP), a selective inhibitor of CaMKII. Arterial smooth muscle cells express a robust CaMKII-activated Cl– conductance; however, CLC-3–/– cells did not. The N-terminus of CLC-3, which contains a CaMKII consensus sequence, was phosphorylated by CaMKII in vitro, and mutation of the serine at position 109 (S109A) abolished the CaMKII-dependent Cl– conductance, indicating that this residue is important in the gating of CLC-3 at the plasma membrane.
(Received 12 November 2003;
accepted after revision 28 January 2004;
first published online 30 January 2004)
Corresponding author D. J. Nelson: Department of Neurobiology, Pharmacology, and Physiology, The University of Chicago, 947 East 58th Street, AB-500 MC-0926, Chicago, IL 60637, USA. Email: dnelson{at}drugs.bsd.uchicago.edu
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