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J Biol Chem, Vol. 275, Issue 13, 9725-9733, March 31, 2000
From the Departments of Little is known about the role of Rho proteins in
apoptosis produced by stimuli evolved specifically to produce
apoptosis, such as granzymes from cytotoxic T lymphocytes (CTLs) and
Fas. Here we demonstrate that all three Rho family members are involved in CTL- and Fas-induced killing. Dominant-negative mutants of each Rho
family member and Clostridium difficile toxin B, an
inhibitor of all family members, strongly inhibited the susceptibility
of cells to CTL- and Fas-induced apoptosis. Fas-induced caspase-3 activation was inhibited by C. difficile toxin. Activated
mutants of each GTPase increased susceptibility to apoptosis, and
activation of Cdc42 increased within 5 min of Fas stimulation. In
contrast, during the time required for CTL and Fas killing, no
apoptosis was produced by dominant-negative or activated mutants or by
C. difficile toxin alone. Inhibition of actin
polymerization using latrunculin A reduced the ability of
constitutively active GTPase mutants to stimulate apoptosis and blocked
Fas-induced activation of caspase-3. Furthermore, the ability of Rac to
enhance apoptosis was decreased by point mutations reported to block
Rac induction of actin polymerization. Rho family proteins may regulate
apoptosis through their effects on the actin cytoskeleton.
Rho Family Proteins Modulate Rapid Apoptosis Induced by Cytotoxic
T Lymphocytes and Fas*
,¶,,
,¶, and**
Cell Biology and
¶ Immunology and the § Neuropharmacology Department,
Division of Virology, Scripps Research Institute, La Jolla, California
92037 and Chiron Corporation,
Emeryville, California 94608-2916
*
This work was supported by the National Institutes of Health
Grant R01 AG15430. This is Manuscript 11800CB from the Scripps Research
Institute.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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