Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with Ras in activating extracellular signal-regulated kinase ERK1.

@article{Recio2000BothNA,
  title={Both normal and transforming PCPH proteins have guanosine diphosphatase activity but only the oncoprotein cooperates with Ras in activating extracellular signal-regulated kinase ERK1.},
  author={Juan Angel Recio and J. Guillermo P{\'a}ez and Baishali Maskeri and Mark Loveland and J A M{\'e}rida Velasco and Vicente Notario},
  journal={Cancer research},
  year={2000},
  volume={60 6},
  pages={1720-8}
}
Previous reports from our laboratory described the activation of the PCPH gene into the PCPH oncogene (mt-PCPH, reported previously as Cph) by a single point mutational deletion. As a consequence, the mt-PCPH oncoprotein is a truncated form of the normal PCPH protein. Although both proteins have ribonucleotide diphosphate-binding activity, only mt-PCPH acted synergistically with a human H-Ras oncoprotein to transform murine NIH3T3 fibroblasts. We report here the expression of the PCPH and mt… CONTINUE READING

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Cross - talk between Smad 1 and Ras / MEK signaling pathways for TGF b

  • X. Li, J. W. Lee, L. M. Graves, H. S. Earp
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  • 1999

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