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J Biol Chem. 2002 Jun 21;277(25):22798-805. Epub 2002 Apr 4.

c-Src-dependent transcriptional activation of TFII-I.

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  • 1Department of Pathology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.


TFII-I is a multifunctional transcription factor that is also involved in signal transduction. Here we show that TFII-I undergoes a c-Src-dependent tyrosine phosphorylation on tyrosine residues 248 and 611 and translocates to the nucleus in response to growth factor signaling. Tyrosine-phosphorylated nuclear TFII-I activates a stably integrated c-fos reporter gene. Withdrawal of signal leads to diminution of nuclear TFII-I, suggesting that the signal-dependent translocation is reversible. Antibodies against either TFII-I or c-Src abrogate growth factor-stimulated activation of c-fos. Consistent with the notion that tyrosine phosphorylation of TFII-I is required for its transcriptional activity, phosphorylation-deficient mutants of TFII-I fail to activate the c-fos promoter. These data demonstrate that TFII-I, through a Src-dependent mechanism, reversibly translocates from the cytoplasm to the nucleus, leading to the transcriptional activation of growth-regulated genes.

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