title: Initiation of Xenopus oocyte maturation by activation of the mitogen-activated protein kinase cascade.
abstract: Mitogen-activated protein kinase (MAPK) and MAPK kinase (MAPKK) are activated during Xenopus oocyte maturation concomitant with the activation of maturation promoting factor (MPF). We reported previously that an anti-MAPKK neutralizing antibody inhibited progesterone- or Mos- induced initiation of oocyte maturation. Here, we show that the injection of CL100 (also called MAPK phosphatase-1) into immature oocytes inhibited progesterone-induced oocyte maturation as well as MAPK activation and that injection of mRNA encoding a constitutively active MAPKK induced activation of histone H1 kinase and germinal vesicle breakdown in the absence of progesterone. Injection of recombinant STE11 protein (a yeast MAPKK kinase) also induced initiation of oocyte maturation. These data support the idea that the MAPKK/MAPK cascade plays an important role in oocyte maturation. Interestingly, injection of the active MAPKK mRNA or the STE11 protein resulted in induction and accumulation of Mos protein. Furthermore, in the presence of cycloheximide, the STE11-induced activation of MPF as well as the induction and accumulation of Mos was blocked, and the activation of MAPK was greatly reduced. The increase in Mos protein and the activation of MAPK by injecting cyclin A protein into immature oocytes were both blocked also by cycloheximide treatment. These results are consistent with an idea that there may exist a positive feedback loop consisting of Mos, the MAPKK/MAPK cascade, and MPF, which may be important for the initiation of oocyte maturation induced by progesterone.
authors.affiliation: Department of Genetics and Molecular Biology, Kyoto University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Gotoh
authors.forename: N
authors.initials: N
authors.lastname: Masuyama
authors.forename: K
authors.initials: K
authors.lastname: Dell
authors.forename: K
authors.initials: K
authors.lastname: Shirakabe
authors.forename: E
authors.initials: E
authors.lastname: Nishida
mesh_terms: D000818:Animals; D000906:Antibodies / Q000494:pharmacology; D001483:Base Sequence; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000276:immunology / Q000378:metabolism*; D018797:Cell Cycle Proteins; D002454:Cell Differentiation; D054638:Dual Specificity Phosphatase 1; D004789:Enzyme Activation; D005246:Feedback; D005260:Female; D017874:Immediate-Early Proteins / Q000378:metabolism*; D016200:Maturation-Promoting Factor / Q000378:metabolism; D020929:Mitogen-Activated Protein Kinase Kinases; D008969:Molecular Sequence Data; D009865:Oocytes / Q000254:growth & development*; D010749:Phosphoprotein Phosphatases; D011494:Protein Kinases / Q000378:metabolism; D054645:Protein Phosphatase 1; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D017231:Proto-Oncogene Proteins c-mos / Q000378:metabolism; D015398:Signal Transduction; D014981:Xenopus
chemical_list: D000906:Antibodies; D018797:Cell Cycle Proteins; D017874:Immediate-Early Proteins; D011494:Protein Kinases; D017231:Proto-Oncogene Proteins c-mos; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D016200:Maturation-Promoting Factor; D020929:Mitogen-Activated Protein Kinase Kinases; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; D054638:Dual Specificity Phosphatase 1; D017027:Protein Tyrosine Phosphatases