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J. Biol. Chem., Vol. 269, Issue 11, 7957-7962, Mar, 1994
J Chen, S Parsons and DL Brautigan
The catalytic subunit of protein phosphatase 2A (PP2A) is inactivated by in
vitro phosphorylation of Tyr307 by receptor and nonreceptor protein
tyrosine kinases (Chen, J., Martin, B. L., and Brautigan, D. L. (1992)
Science 257, 1261-1264). Here we show the phosphorylation of PP2A in cells
under different growth conditions. In lysates of nontransformed murine
10T1/2 fibroblasts, there were two forms of PP2A at 36 kDa detected after
two-dimensional gel electrophoresis and immunoblotting with anti-PP2A
peptide antibody. These two forms exactly comigrated with unphosphorylated
purified PP2A and the PP2A 32P-labeled by in vitro phosphorylation with
p60v-src kinase. The phosphorylated form of PP2A recovered from red blood
cells or produced by in vitro phosphorylation was eliminated by incubation
with tyrosine-specific phosphatase (PTP1B). Transformation of 10T1/2 cells
by expression of p60v-src resulted in most of the PP2A in the cells being
converted to a phosphorylated form that was reactive with
anti-phosphotyrosine antibody. Serum starvation of cells reduced the amount
of phosphorylated PP2A, whereas serum stimulation of quiescent cells caused
an increase to the same relative amount of phosphorylated PP2A as in
src-transformed cells. Addition of epidermal growth factor to quiescent
NeoR cells (10T1/2 fibroblasts overexpressing epidermal growth factor
receptors) temporarily increased the level of phosphorylation of PP2A, with
a peak at 5-15 min and a return to basal level within 60 min. The results
show that PP2A is phosphorylated in intact cells, and the extent of this
modification is increased by growth factors or cell transformation,
providing evidence for a physiological mechanism of PP2A regulation.
Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts
Section of Biochemistry, Brown University, Providence, Rhode Island 02912.
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