title: Regulation of the G2/M transition in oocytes of xenopus tropicalis.
abstract: The molecular events regulating hormone-induced oocyte activation and meiotic maturation are probably best understood in Xenopus laevis. In X. laevis, progesterone activates the G2-arrested oocyte, induces entry into M phase of meiosis I (MI) and resumption of the meiotic cell cycles, and leads to the formation of a mature, fertilizable egg. Oocytes of Xenopus tropicalis offer several practical advantages over those of X. laevis, including faster and more synchronous meiotic cell cycle progression, less seasonal variability, and the availability of transgenic approaches. Previous work found several similarities in the pathways regulating oocyte maturation in the two species. Here, we report several additional ones that are conserved in X. tropicalis. (1). Injection of Mos mRNA into G2-arrested oocytes activates the MAP kinase cascade and induces the G2/MI transition. (2). Injection of the beta subunit of the kinase CK2 (a negative regulator of Mos and oocyte activation) delays the G2/MI transition. (3). Elevating PKA activity blocks progesterone-induced maturation; repressing PKA activity induces entry into MI in the absence of progesterone. (4). LF (anthrax lethal factor), which cleaves certain MAP kinase kinases, strongly reduces both the rate and extent of entry into MI. In contrast to the one previously reported major difference between oocytes of the two species, we find that injection of egg cytoplasm ("MPF activity") into G2-arrested X. tropicalis oocytes induces entry into meiosis I even when protein synthesis is blocked, just as it does in oocytes of X. laevis. These results indicate that much of what we have learned from studies of X. laevis oocytes holds for those of X. tropicalis, and suggest that X. tropicalis oocytes offer a good experimental system for investigating certain questions that require a rapid, synchronous progression through the G2/meiosis I transition.
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Jennifer S
authors.initials: JS
authors.lastname: Stanford
authors.forename: Soyan Leung
authors.initials: SL
authors.lastname: Lieberman
authors.forename: Valerie L
authors.initials: VL
authors.lastname: Wong
authors.forename: Joan V
authors.initials: JV
authors.lastname: Ruderman
mesh_terms: D000818:Animals; D000942:Antigens, Bacterial; D001427:Bacterial Toxins / Q000494:pharmacology; D047390:Casein Kinase II; D017868:Cyclic AMP-Dependent Protein Kinases / Q000235:genetics / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D005260:Female; D016195:G2 Phase / Q000187:drug effects / Q000502:physiology*; D008938:Mitosis / Q000187:drug effects / Q000502:physiology*; D017232:Oncogene Proteins v-mos / Q000235:genetics / Q000378:metabolism; D009865:Oocytes / Q000166:cytology* / Q000187:drug effects / Q000502:physiology; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D014981:Xenopus; D029867:Xenopus Proteins / Q000235:genetics / Q000378:metabolism
chemical_list: D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D017232:Oncogene Proteins v-mos; D029867:Xenopus Proteins; C030325:anthrax toxin; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D017868:Cyclic AMP-Dependent Protein Kinases