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J Biol Chem, Vol. 273, Issue 19, 11596-11604, May 8, 1998
From the Howard Hughes Medical Institute and the Department of
Molecular Physiology and Biophysics, Vanderbilt University School of
Medicine, Nashville, Tennessee 37232
Phospholipase D (PLD) has been identified
as a target of small G proteins of the Rho family. The present study
was directed at defining the interaction sites of RhoA with rat brain
PLD in vitro using chimeric proteins between RhoA and
Ha-Ras or Cdc42Hs and point mutations.
The switch I region of RhoA, which is the common effector domain of
Ras-like G proteins, was a crucial interaction site for PLD. Mutations
in conserved amino acids (Tyr34, Thr37,
Phe39) totally abolished PLD activation, while mutations in
Val38 or Tyr42 caused partial loss. Two
additional sites were responsible for the differential PLD activation
ability between RhoA and Cdc42Hs. Changing Asp76 in the
switch II region of RhoA to the corresponding amino acid in Cdc42Hs led
to partial loss of PLD activation. A chimeric protein with the
N-terminal third of Cdc42Hs changed to RhoA showed enhanced PLD
activation. Analysis of other Rho/Ha-Ras chimeric proteins and
mutations indicated that Gln52 adjacent to the switch II
region is responsible for this gain of function.
In conclusion, the present study shows that conserved amino acids in
the switch I region of RhoA are major PLD interaction sites and that
residues in the switch II and internal regions are responsible for the
differential activation of PLD by RhoA and Cdc42Hs.
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