Title : The PCPH oncoprotein antagonizes the proapoptotic role of the mammalian target of rapamycin in the response of normal fibroblasts to ionizing radiation.

Pub. Date : 2003 Oct 1

PMID : 14559816






3 Functional Relationships(s)
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1 The same IR doses that activated mTOR induced the phosphorylation of p53 on Ser(18) (mouse equivalent to human Ser(15)) and the subsequent transcriptional activation of PUMA, a known proapoptotic p53-target gene, and promoted apoptosis involving increased overall caspase activity, caspase-3 activation, cleavage of poly(ADP-ribose) polymerase (PARP) and classic protein kinase C (PKC) isoforms, and DNA fragmentation. Serine mechanistic target of rapamycin kinase Mus musculus
2 The same IR doses that activated mTOR induced the phosphorylation of p53 on Ser(18) (mouse equivalent to human Ser(15)) and the subsequent transcriptional activation of PUMA, a known proapoptotic p53-target gene, and promoted apoptosis involving increased overall caspase activity, caspase-3 activation, cleavage of poly(ADP-ribose) polymerase (PARP) and classic protein kinase C (PKC) isoforms, and DNA fragmentation. Serine mechanistic target of rapamycin kinase Mus musculus
3 Furthermore, the proapoptotic function of mTOR was also antagonized by the expression in MEF3T3 cells of the PCPH oncoprotein, known to enhance cell survival by causing partial ATP depletion. Adenosine Triphosphate mechanistic target of rapamycin kinase Mus musculus