IMR Press / FBL / Volume 11 / Issue 3 / DOI: 10.2741/1979

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


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

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1 Molecular Cardiology, New York Harbor VA Medical Center, 800 Poly Place, Brooklyn, NY 11209
2 QRNA Corporation, West 167th Street, New York, NY 10032
3 Columbia College of Physicians and Surgeons, 630 West 168th Street, New York, NY 10032
4 Department of Pharmacology & Biological Chemistry and the Microarray Research Facility, Mount Sinai Medical Center, 1 Gustave Levy Place, Box 1603, New York, NY 10029
5 Department of Medicine, New York Harbor VA Medical Center, 800 Poly Place, Brooklyn, NY 11209
6 Department of Pathology, SUNY Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, NY 11203
7 Department of Microbiology and Human Genetics, Robert Wood Johnson Medical Center, University of Medicine and Dentistry of New Jersey, 675 Hoes Lane – Room 727, Piscataway, NJ 08854
8 Cancer Institute of New Jersey, New Brunswick, NJ 08901
9 Departments of Physiology and Pharmacology, SUNY Downstate Medical Center, 450 Clarkson Avenue, Brooklyn, NY 11203
10 Department of Pathology & Laboratory Medicine, New York Harbor VA Medical Center, 800 Poly Lace, Brooklyn, NY 11209
Front. Biosci. (Landmark Ed) 2006, 11(3), 2420–2427;
Published: 1 September 2006

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.

gene array
Oncogenic Ras-P21
Insulin-Activated Wild-Type Ras-P21
Oocyte Maturation
Gene Expression
Protein Expression
Dual Specificity Kinase
Signal Transduction Pathways
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