Stimulation of Kv1.3 potassium channels by death receptors during apoptosis in Jurkat T lymphocytes

doi:10.1074/jbc.M300443200

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Papers In Press, published online ahead of print June 15, 2003
J. Biol. Chem, 10.1074/jbc.M300443200
Submitted on January 15, 2003
Revised on May 22, 2003
Accepted on June 15, 2003

Stimulation of Kv1.3 potassium channels by death receptors during apoptosis in Jurkat T lymphocytes

Nina M. Storey, Mireia Gomez-Angelats, Carl D. Bortner, David L. Armstrong, and John A. Cidlowski

Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709

Corresponding Author: storey{at}niehs.nih.gov

The loss of intracellular potassium is a pivotal step in the induction of apoptosis but the mechanisms underlying this response are poorly understood. Here we report caspase-dependant stimulation of potassium channels by the Fas receptor in a human Jurkat T cell line. Receptor activation with Fas ligand for 30 minutes increased the amplitude of voltage-activated potassium currents two fold on average. This produces a sustained outward current, ~10 pA, at physiological membrane potentials during Fas ligand- induced apoptosis. Both basal and Fas ligand-induced currents were blocked completely by toxins that selectively inhibit Kv1.3 potassium channels. Kv1.3 stimulation required the expression of Fas-associated death domain (FADD) protein and activation of caspase 8, but did not require activation of caspase 3 or protein synthesis. Furthermore, Kv1.3 stimulation by Fas ligand was prevented by chronic stimulation of protein kinase C with 20 nM phorbol 12-myristate 13-acetate (PMA) during Fas ligand treatment, which also blocks apoptosis. Thus, Fas ligand increases Kv1.3 channel activity through the same canonical apoptotic signaling cascade that is required for potassium efflux, cell shrinkage and apoptosis.

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