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J Biol Chem, Vol. 273, Issue 8, 4392-4399, February 20, 1998
,§,, and
From the Departments of Aluminum tetrafluoride
(AlF4 Pharmacology and
§ Chemistry, Cornell University,
Ithaca, New York 14853
)
activation of heterotrimeric G-protein 
-subunits is a well
established aspect of the biochemistry of these proteins; however,
until recently it has been thought that
AlF4
does not mediate effects on the Ras superfamily of low molecular weight
GTP-binding proteins. Recent work demonstrating aluminum fluoride-induced complex formation between Ras and its
GTPase-activating proteins (RasGAP and NF1) has provided important
insights into the mechanism of GAP-stimulated GTP hydrolysis. We have
characterized the
AlF4-induced
complex formation between the GDP-bound form of the Rho subfamily
G-protein Cdc42Hs and a limit functional domain of the Cdc42-GAP using
a variety of biochemical techniques. Our results indicate that the
apparent affinity of GAP for the
AlF4-mediated
complex is similar to the affinity observed for the activated
(GTP-bound) form of Cdc42 and that beryllium (Be) can replace aluminum
in mediating fluoride-induced complex formation. Additionally, the
AlF4-induced
interaction is weakened significantly by the catalytically compromised GAP(R305A) mutant, indicating that this arginine is critical in transition state stabilization. Unlike Ras, we find that
AlF4
and
BeF3
mediate complex formation between Cdc42Hs·GDP and downstream target/effector molecules, indicating that there are important differences in the mechanism of effector binding between the Ras and
Rho subfamily G-proteins.
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