CaT1 manifests the pore properties of the calcium-release-activated calcium channel

Lixia Yue, Ji-Bin Peng, Matthias A. Hediger and David E. Clapham ()
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Lixia Yue: Children's Hospital, Harvard Medical School, Enders 1309
Ji-Bin Peng: Brigham and Women's Hospital and Harvard Medical School
Matthias A. Hediger: Brigham and Women's Hospital and Harvard Medical School
David E. Clapham: Howard Hughes Medical Institute

Nature, 2001, vol. 410, issue 6829, 705-709

Abstract: Abstract The calcium-release-activated Ca2+channel, ICRAC1,2,3, is a highly Ca2+-selective ion channel that is activated on depletion of either intracellular Ca2+ levels or intracellular Ca2+ stores. The unique gating of ICRAC has made it a favourite target of investigation for new signal transduction mechanisms; however, without molecular identification of the channel protein, such studies have been inconclusive. Here we show that the protein CaT1 (ref. 4), which has six membrane-spanning domains, exhibits the unique biophysical properties of ICRAC when expressed in mammalian cells. Like ICRAC, expressed CaT1 protein is Ca2+ selective, activated by a reduction in intracellular Ca2+ concentration, and inactivated by higher intracellular concentrations of Ca2+. The channel is indistinguishable from ICRAC in the following features: sequence of selectivity to divalent cations; an anomalous mole fraction effect; whole-cell current kinetics; block by lanthanum; loss of selectivity in the absence of divalent cations; and single-channel conductance to Na+ in divalent-ion-free conditions. CaT1 is activated by both passive and active depletion of calcium stores. We propose that CaT1 comprises all or part of the ICRAC pore.

Date: 2001
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DOI: 10.1038/35070596

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