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J. Biol. Chem., Vol. 268, Issue 5, 3494-3498, 02, 1993
KM Lounsbury, B Schlegel, M Poncz, LF Brass and DR Manning
The G protein alpha subunit Gz alpha is a substrate for phosphorylation by
protein kinase C. The phosphorylation has been documented both in human
platelets and in vitro and is characterized by a high degree of selectivity
in relation to other G protein alpha subunits. We have demonstrated
previously by phosphoamino acid analysis and CNBr peptide mapping that
phosphorylation occurs at a serine residue(s) within the NH2-terminal 53
residues of Gz alpha. In this study, we have examined the site of
phosphorylation using site-directed mutagenesis. Gz alpha variants
containing selected substitutions of alanine for serine residues were
expressed in human kidney 293 cells, and the ability of each to be
phosphorylated in response to phorbol 12-myristate 13- acetate was
examined. A focus was placed on Ser25 and Ser27, the 2 serine residues
within a sequence of Gz alpha used to obtain a phosphorylation-sensitive
antibody. The results demonstrate that Ser27 is the primary site of
phosphorylation. Conversion of Ser27 to an alanine resulted in a 65%
decrease in incorporation of [32P] phosphate; conversion of Ser25 had no
effect. Conversion of Ser16, which like Ser25 and Ser27 conforms to a
consensus site for protein kinase C, resulted in a modest (15%) decrease.
The conversion of both Ser16 and Ser27 resulted in an 80% suppression of
incorporation. In addition to these results, we have extended studies of
the subunit and kinase selectivity of phosphorylation in platelets. We show
here that under conditions promoting phorbol 12-myristate
13-acetate-stimulated phosphorylation of Gz alpha in permeabilized
platelets, Gq alpha is not phosphorylated. Moreover, Gi alpha, Gz alpha,
and Gq alpha were not phosphorylated in response to analogues of cAMP or
cGMP. Thus, only Gz alpha is phosphorylated in platelets and only in
response to activation of protein kinase C.
Analysis of Gz alpha by site-directed mutagenesis. Sites and specificity of protein kinase C-dependent phosphorylation
Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia.
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