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J Biol Chem, Vol. 273, Issue 35, 22554-22562, August 28, 1998
,,, and§
From the Dramatic transient changes resulting in a
stellate morphology are induced in many cell types on treatment with
agents that enhance intracellular cAMP levels. Thrombin fully protects
cells from this inductive effect of cAMP through the thrombin receptor. The protective effect of thrombin was shown to be
Rho-dependent. Clostridium botulinum C3
exoenzyme, which inactivates RhoA functions, abolished the ability of
thrombin to protect cells from responding to increased cAMP levels. A
constitutively activated RhoAV14 mutant protein also
prevented cells from responding to cAMP. RhoA can be specifically
phosphorylated at Ser-188 by the cAMP-activated protein kinase A (PKA).
We demonstrate that RhoAV14A188, which cannot be
phosphorylated by PKA in vitro, is more effective than
RhoAV14 in preventing cells from responding to cAMP and in
inducing actin stress fiber formation. This suggests that PKA
phosphorylation of RhoA impairs its biological activity in
vivo. ROK Glaxo-IMCB Group, Institute of Molecular and
Cell Biology, 30 Medical Drive, Singapore 117609 and
§ Institute of Neurology, University College London, 1 Wakefield Street, London WC1N 1PJ, United Kingdom
, a RhoA-associated serine/threonine kinase can also
prevent cells from responding to cAMP with shape changes.
Phosphorylation of RhoA by PKA in vitro decreases the
binding of RhoA to ROK. These results indicate that RhoA and cAMP
have antagonistic roles in regulating cellular morphology and suggest
that cAMP-mediated down-regulation of RhoA binding to its effector
ROK may be involved in this antagonism.
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