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J. Biol. Chem., Vol. 269, Issue 6, 4565-4570, Feb, 1994
S Kamada, K Toyoshima and T Akiyama
To understand the mechanisms regulating the transactivating activity of
Jun/AP-1, we analyzed alterations in c-Jun induced by growth stimulation
and cell transformation. Serum stimulation of quiescent NIH3T3 cells
induced a marked increase in phosphorylation of c-Jun in its amino-terminal
activation domain. On the other hand, this domain was highly
phosphorylated, in a serum-independent manner, in cells transformed with
various oncogenes, including active c-raf-1, v-src, active Ha-ras, and
active erbB-2. There were no obvious differences in the phosphorylation
states of c-Jun in exponentially growing normal and transformed cells.
However, in the exponentially growing state, the TRECAT activity in
transformed cells was markedly higher than that in normal cells. Gel
retardation analysis indicated that the AP-1 components in transformed
cells were significantly different from those in normal cells. These
results suggest that some other alterations besides phosphorylation of
c-Jun are involved in enhancement of AP-1 activity in exponentially growing
transformed cells.
Serum-independent phosphorylation of c-Jun and alterations in AP-1 components by transformation with various oncogenes
Department of Oncogene Research, Osaka University, Japan.
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