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J. Biol. Chem., Vol. 276, Issue 51, 47767-47770, December 21, 2001
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From the The calcium release-activated calcium
channel (CRAC) is a highly Ca2+-selective ion channel
that is activated on depletion of inositol triphosphate
(IP3)-sensitive intracellular Ca2+ stores. It
was recently reported that CaT1, a member of the TRP family of cation
channels, exhibits the unique biophysical properties of CRAC, which led
to the conclusion that CaT1 comprises all or part of the CRAC pore
(Yue, L., Peng, J. B., Hediger, M. A., and Clapham, D. E. (2001) Nature 410, 705-709). Here, we directly compare
endogenous CRAC with heterologously expressed CaT1 and show that they
manifest several clearly distinct properties. CaT1 can be distinguished
from CRAC in the following features: sensitivity to store-depleting
agents; inward rectification in the absence of divalent cations;
relative permeability to Na+ and Cs+; effect of
2-aminoethoxydiphenyl borate (2-APB). Moreover, CaT1 displays a mode of
voltage-dependent gating that is fully absent in CRAC and
originates from the voltage-dependent binding/unbinding of
Mg2+ inside the channel pore. Our results imply that the
pores of CaT1 and CRAC are not identical and indicate that CaT1 is a
Mg2+-gated channel not directly related to CRAC.
Laboratory of Physiology, Catholic
University of Leuven, B-3000 Leuven, Belgium, ¶ Laboratory of Cell
and Molecular Signalling, Center for Biomedical Research, The Queen's
Medical Center and John A. Burns School of Medicine, University
of Hawaii, Honolulu, Hawaii 96813, and the Department of Cell
Physiology, Institute of Cellular Signalling, University Medical Centre
of Nijmegen, Nijmegen, The Netherlands
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M. Prakriya and R. S. Lewis Separation and Characterization of Currents through Store-operated CRAC Channels and Mg2+-inhibited Cation (MIC) Channels J. Gen. Physiol., April 29, 2002; 119(5): 487 - 508. [Abstract] [Full Text] [PDF]
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