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Middle tumor antigen (MT) is the primary transforming protein of
murine Polyomavirus. MT transforms by associating with and
modulating the activities of cellular proteins involved in control of
cell proliferation. MT binds to and is phosphorylated by cellular
tyrosine kinases. The phosphorylated tyrosines become docking sites for
SH2 (Src homology 2) domain-containing molecules. Tyrosine 322 of MT is
known to be phosphorylated but has no known binding protein. We have
found that phospholipase C-
Volume 270,
Number 21,
Issue of May 26, pp. 12331-12334, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
1
1 (PLC-
1), a SH2 domain-containing
protein, coimmunoprecipitates with MT. Tyrosine phosphorylation of
PLC-
1 is elevated in cells expressing MT, suggesting activation of
this enzyme by MT. A Tyr-322
Phe mutation in MT renders it
defective in MT-PLC-
1 interaction and in transformation. From the
correlation between transformation and MT-PLC-
1 interaction, we
suggest that PLC-
1 may play a role in transformation.
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