Two dual specificity kinases are preferentially induced by wild-type rather than by oncogenic RAS-P21 in Xenopus oocytes

Front Biosci. 2006 Sep 1;11:2420-7. doi: 10.2741/1979.


In prior studies, we have found that oncogenic ras-p21 protein induces oocyte maturation using pathways that differ from those activated by insulin-induced wild-type ras-p21. Both oncogenic and wild-type ras-p21 require interactions with raf, but unlike oncogenic ras-p21, insulin-activated wild-type ras-p21 does not depend completely on activation of MEK and MAP kinase (MAPK or ERK) on the raf kinase pathway. To determine what raf-dependent but MAPK-independent pathway is activated by wild-type ras-p21, we have analyzed gene expression in oocytes induced to mature either with oncogenic ras-p21 or with insulin using a newly available Xenopus gene array. We find a number of proteins that are preferentially expressed in one or the other system. Of these, two proteins, both dual function kinases, T-Cell Origin Protein Kinase (TOPK) and the nuclear kinase, DYRK1A, are preferentially expressed in the insulin system. Confirming this finding, blots of lysates of oocytes, induced to mature with oncogenic ras-p21 and insulin, with anti-TOPK and anti-DYRK1A show much higher protein expression in the lysates from the insulin-matured oocytes. Neither of these kinases activates or is activated by MAPK and is therefore an attractive candidate for being on a signal transduction pathway that is unique to insulin-activated wild-type ras-p21-induced oocyte maturation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Blotting, Western
  • Cell Cycle / physiology
  • Enzyme Induction
  • Female
  • Gene Expression Profiling*
  • Insulin / physiology*
  • JNK Mitogen-Activated Protein Kinases / biosynthesis
  • Mitogen-Activated Protein Kinase Kinases
  • Mitogen-Activated Protein Kinases / biosynthesis
  • Oligonucleotide Array Sequence Analysis
  • Oocytes / metabolism*
  • Protein Serine-Threonine Kinases / biosynthesis*
  • Protein-Tyrosine Kinases / biosynthesis*
  • Proto-Oncogene Proteins p21(ras) / physiology*
  • Signal Transduction
  • Xenopus Proteins / biosynthesis*
  • Xenopus laevis


  • Insulin
  • Xenopus Proteins
  • Dyrk kinase
  • Protein-Tyrosine Kinases
  • PBK protein, Xenopus
  • Protein Serine-Threonine Kinases
  • JNK Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinases
  • Mitogen-Activated Protein Kinase Kinases
  • Proto-Oncogene Proteins p21(ras)