Phosphorylation of H-ras proteins by protein kinase A

  • Arimura S
  • Nakata H
  • Tomiyama K
 et al. 
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Abstract

Protein phosphorylation is one of several representative post translational modifications. Cyclic AMP-dependent protein kinase (PKA) plays the crucial and varying role of signal transduction. On the other hand, ras protein plays an important role in cell proliferation and growth. Although a previous report showed that H-ras protein was phosphorylated by PKA, the stiochiometry was not determined, so we investigated the stoichiometry of phosphorylation of the protein by PKA. H-ras cDNA inserted into a pGEX-2T expressing vector produced high levels of recombinant H-ras (rH-ras) in a fusion protein with glutathione S-transferase. rH-ras was obtained after cleavage by thrombin. Phosphorylation of ras protein by the catalytic subunit of PKA was performed, and the radioactivity was counted after SDS-PAGE and autoradiography. The results indicate that less than 0.1 mol of phosphate was incorporated per mol of H-ras protein, and suggest that H-ras protein could not be a physiologically meaningful substrate for PKA.

Author-supplied keywords

  • H-ras
  • Phosphorylation
  • Protein kinase A

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Authors

  • Shinya Arimura

  • Hiroko Nakata

  • Koji Tomiyama

  • Yasuhiro Watanabe

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