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J Biol Chem, Vol. 274, Issue 1, 48-51, January 1, 1999
From the Department of Physiology II, Kobe University School of
Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan
Rap1A is phosphorylated by
cAMP-dependent protein kinase (PKA), and this
phosphorylation has been shown to modulate its interaction with other
proteins. However, it is not known whether Rap1A phosphorylation is
involved in regulation of its cellular functions, including suppression
of Ras-dependent Raf-1 activation. We have previously shown
that this suppressive activity of Rap1A is attributable to its greatly
enhanced ability to bind to the cysteine-rich region (CRR, residues
152-184) of Raf-1 compared with that of Ras. Here, we show that
phosphorylation of Rap1A by PKA abolished its binding activity to CRR.
Furthermore, a mutant Rap1A(S180E), whose sole PKA phosphorylation
residue, Ser-180, was substituted by an acidic residue, Glu, to mimic
its phosphorylated form, failed to suppress Ras-dependent
Raf-1 activation in COS-7 cells. These results indicate that the CRR
binding activity and the Ras-suppressive function of Rap1A can be
modulated through phosphorylation and suggest that Rap1A may function
as a PKA-dependent regulator of Raf-1 activation, not
merely as a suppressor.
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