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Phosphorylation Site
(Received for publication, June 28, 1996)
,
From the Laboratory of Cellular and Molecular Biology, National
Cancer Institute, Bethesda, Maryland 20892, § Ben May
Institute for Cancer Research and Department of Pharmacological and
Physiological Sciences, the University of Chicago, Chicago Illinois
60637, and Protein kinase C-
NHLBI, National Institutes of Health,
Bethesda, Maryland 20892
(PKC-) has been
demonstrated to be phosphorylated on tyrosine residue(s) in many
different biological systems (Li, W., Yu, J.-C., Michieli, P., Beeler,
J. F., Ellmore, N., Heidaran, M. A., and Pierce, J. H. (1994)
Mol. Cell. Biol. 14, 6727-6735; Li, W., Mischak, H., Yu,
J.-C., Wang, L.-M., Mushinski, J. F., Heidaran, M. A., and Pierce, J. H. (1994) J. Biol. Chem. 269, 2349-2352; Denning, M. F., Dlugosz, A. A., Howett, M. A., and Yuspa, S. H. (1993)
J. Biol. Chem. 268, 26079-26081). Tyrosine
phosphorylation of PKC- has also been shown to occur in
vitro when purified PKC- is coincubated with different
tyrosine kinase sources. However, the tyrosine phosphorylation site(s)
is currently unknown and the exact effect of this phosphorylation on
its serine/threonine kinase activity and biological functions is still
controversial. To directly investigate the potential role of PKC-
tyrosine phosphorylation, tyrosine 187 was converted to phenylalanine
(PKC-Y187F) by site-directed mutagenesis, and expression vectors
containing PKC-Y187F cDNAs were transfected into both 32D
myeloid progenitor cells and NIH 3T3 fibroblasts. The results showed
that tyrosine 187 of PKC- became phosphorylated in vivo
in response to 12-O-tetradecanoylphorbol-13-acetate
stimulation or platelet-derived growth factor receptor activation.
In vivo labeling and subsequent two-dimensional
phosphopeptide analysis demonstrated that one phosphopeptide was absent
in PKC-Y187F when compared to wild type PKC-, further
substantiating that tyrosine 187 of PKC- is phosphorylated in
vivo. Although the phosphotyrosine content of PKC-Y187F was
reduced compared with PKC-WT, the kinase activity of PKC-Y187F
toward a PKC- substrate was not altered. Moreover,
12-O-tetradecanoylphorbol-13-acetate-mediated monocytic
differentiation of 32D cells was not affected by expression of the
PKC-Y187F mutant. Taken together, these results suggest that
tyrosine phosphorylation of PKC- on 187 may not influence PKC-
activation and known functions.
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