title: Two dual specificity kinases are preferentially induced by wild-type rather than by oncogenic RAS-P21 in Xenopus oocytes.
abstract: 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.
authors.affiliation: Molecular Cardiology, New York Harbor VA Medical Center, Brooklyn, NY 11209, USA.
authors.forename: Yongxia
authors.initials: Y
authors.lastname: Qu
authors.forename: Victor
authors.initials: V
authors.lastname: Adler
authors.forename: Tearina
authors.initials: T
authors.lastname: Chu
authors.forename: Ovidu
authors.initials: O
authors.lastname: Platica
authors.forename: Josef
authors.initials: J
authors.lastname: Michl
authors.forename: Sidney
authors.initials: S
authors.lastname: Pestka
authors.forename: Lara
authors.initials: L
authors.lastname: Izotova
authors.forename: Mohamed
authors.initials: M
authors.lastname: Boutjdir
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Pincus
mesh_terms: D000818:Animals; D015153:Blotting, Western; D002453:Cell Cycle / Q000502:physiology; D004790:Enzyme Induction; D005260:Female; D020869:Gene Expression Profiling; D007328:Insulin / Q000502:physiology*; D048031:JNK Mitogen-Activated Protein Kinases / Q000096:biosynthesis; D020929:Mitogen-Activated Protein Kinase Kinases; D020928:Mitogen-Activated Protein Kinases / Q000096:biosynthesis; D020411:Oligonucleotide Array Sequence Analysis; D009865:Oocytes / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000096:biosynthesis*; D011505:Protein-Tyrosine Kinases / Q000096:biosynthesis*; D016283:Proto-Oncogene Proteins p21(ras) / Q000502:physiology*; D015398:Signal Transduction; D029867:Xenopus Proteins / Q000096:biosynthesis*; D014982:Xenopus laevis; D000097603:Dyrk Kinases
chemical_list: D007328:Insulin; D048031:JNK Mitogen-Activated Protein Kinases; D020929:Mitogen-Activated Protein Kinase Kinases; D020928:Mitogen-Activated Protein Kinases; D017346:Protein Serine-Threonine Kinases; D011505:Protein-Tyrosine Kinases; D016283:Proto-Oncogene Proteins p21(ras); D029867:Xenopus Proteins; D000097603:Dyrk Kinases; C511060:PBK protein, Xenopus