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Vol. 9, Issue 5, 1053-1063, May 1998
and
*Department of Physiology, University College, London WC1E 6BT,
United Kingdom; and
We applied recombinant forms of the Rho-related small guanosine
triphosphatases (GTPases) Rac2 and Cdc42/G25K to permeabilized mast
cells to test their ability to regulate exocytotic secretion. Mast
cells permeabilized with streptolysin-O leak soluble (cytosol) proteins
over a period of 5 min and become refractory to stimulation by
Ca2+ and guanosine triphosphate (GTP)Department of Biological Sciences,
University of Durham, Durham DH1 3LE, United Kingdom
S over about 20-30
min. This loss of sensitivity is likely to be due to loss of key
regulatory proteins that are normally tethered at intracellular
locations. Exogenous proteins that retard this loss of sensitivity to
stimulation may be similar, if not identical, to those secretory
regulators that are lost. Recombinant Rac and Cdc42/G25K, preactivated
by binding GTPS, retard the loss of sensitivity (run-down) and, more
importantly, enable secretion to be stimulated by Ca2+
alone. Investigation of the concentration dependence of each of these
two GTPases applied individually to the permeabilized cells, and of
Cdc42/G25K applied in the presence of an optimal concentration of Rac2,
has provided evidence for a shared effector pathway and also a second
effector pathway activated by Cdc42/G25K alone. Dominant negative
mutant (N17) forms of Rac2 and Cdc42/G25K inhibit secretion induced by
Ca2+ and GTPS. Our data suggest that Rac2 and Cdc42
should be considered as candidates for GE, GTPases that
mediate exocytosis in cells of hematopoeitic origin.
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