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J. Biol. Chem., Vol. 268, Issue 28, 20737-20740, Oct, 1993
C Fasolato, M Hoth and R Penner
Calcium influx in electrically non-excitable cells is regulated by the
filling state of intracellular calcium stores. Depletion of stores
activates plasma membrane channels that are voltage-independent and highly
selective for Ca2+ ions. We report here that the activation of plasma
membrane Ca2+ currents induced by depletion of Ca2+ stores requires a
diffusible cytosolic factor that washes out with time when dialyzing cells
in the whole-cell configuration of the patch-clamp technique. The
activation of calcium release-activated calcium current (ICRAC) by
ionomycin- or inositol 1,4,5-trisphosphate-induced store depletion is
blocked by guanosine 5'-3-O-(thio)triphosphate (GTP gamma S) and
guanyl-5'-yl imidodiphosphate, non-hydrolyzable analogs of GTP, suggesting
the involvement of a GTP-binding protein. The inhibition by GTP gamma S
occurs at a step prior to the activation of ICRAC and is prevented by the
addition of GTP. We conclude that the activation mechanism of
depletion-induced Ca2+ influx encompasses a GTP-dependent step, possibly
involving an as yet unidentified small GTP-binding protein.
A GTP-dependent step in the activation mechanism of capacitative calcium influx
Department of Membrane Biophysics, Max-Planck-Institute for Biophysical Chemistry, Gottingen, Federal Republic of Germany.
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