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J Biol Chem, Vol. 274, Issue 37, 25983-25985, September 10, 1999
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From the Imin is a plasma
membrane-located, Ca2+-selective channel that is activated
by store depletion and regulated by inositol 1,4,5-trisphosphate (IP3). In the present work we examined the coupling between
Imin and IP3 receptors in excised
plasma membrane patches from A431 cells. Imin
was recorded in cell-attached mode and the patches were excised into
medium containing IP3. In about 50% of experiments excision caused the loss of activation of Imin
by IP3. In the remaining patches activation of
Imin by IP3 was lost upon extensive washes of the patch surface. The ability of IP3 to activate
Imin was restored by treating the patches with
rat cerebellar microsomes reach in IP3 receptors but not by
control forebrain microsomes. The re-activated
Imin had the same kinetic properties as
Imin when it is activated by
Ca2+-mobilizing agonists in intact cells and by
IP3 in excised plasma membrane patches and it was inhibited
by the Icrac inhibitor SKF95365. We propose
that Imin is a form of
Icrac and is gated by IP3 receptors.
Institute of Cytology, Russian Academy of
Sciences, St. Petersburg, Russia 194064 and the § Department
of Physiology, University of Texas Southwestern Medical Center,
Dallas, Texas 75235
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