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p53 is an important tumor suppressor that regulates the expression of many genes involved in cell-cycle arrest, DNA repair, and apoptosis. We have previously shown that the tumor suppressor p53 increases the expression of the transcription factor CBP by a mechanism that requires its interaction with the transcription coactivator p300. Here we show that p53 and CBP physically interact with the tumor-suppressive protein tyrosine kinase (TOK1) and we demonstrate that p53 phosphorylates TOK1. The p53-mediated phosphorylation of TOK1 requires its kinase domain and is dependent upon its active form. In addition, we demonstrate that phosphorylation of TOK1 is not sufficient to promote its interaction with CBP or to inhibit the transcriptional activation function of CBP. Phosphorylation of TOK1 did, however, induce the activation of two mitogen-activated protein (MAP) kinases, p38 and c-jun NH(2)-terminal kinase. These results suggest that p53-induced phosphorylation of TOK1 is a mechanism by which p53 activates MAP kinases and p53 inhibits p38-mediated pro-apoptotic signals.Many methods are known in the art for handling data such as XML and related technologies. The first methods took advantage of static hardware that had dedicated circuitry for storing and manipulating XML data. However, these methods are subject to much larger time delays than the present invention. It is believed that the long time delays 0b46394aab
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