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Deciphering the H-Ras pathway in Xenopus oocyte.
Gaffré, M; Dupré, A; Valuckaite, R; Suziedelis, K; Jessus, C; Haccard, O.
Afiliación
  • Gaffré M; Laboratoire de Biologie du Développement, UMR-CNRS 7622, Université Pierre et Marie Curie, Paris, France.
Oncogene ; 25(37): 5155-62, 2006 Aug 24.
Article en En | MEDLINE | ID: mdl-16607282
Xenopus oocytes are arrested in prophase of the first meiotic division. In response to progesterone, they re-enter meiosis and arrest again in metaphase of the second meiotic division. This process, called meiotic maturation, is under the control of the Cyclin B-Cdc2 complex, M phase promoting factor (MPF). Injection of a constitutively active Xenopus H-Ras protein activates MPF, suggesting that Ras proteins could be implicated in the progesterone transduction pathway. The aim of this study was (1) to elucidate the pathway triggered by H-Ras leading to MPF activation in Xenopus oocytes and (2) to investigate whether endogenous H-Ras is involved in the physiological process of meiotic maturation. We generated three constitutively active double mutants, each of them recruiting a single effector in mammalian cells, mitogen-activated protein kinase (MAPK), phosphatidylinositol 3-kinase (PI3K) or RalGDS. Our results show that the activation of a PI3K-related enzyme is crucial for H-Ras-induced MPF activation, whereas the recruitment of either MAPK or RalGDS is not. However, although the H-Ras/PI3K pathway is functional in Xenopus oocytes, it is not the physiological transducer of progesterone responsible for meiotic resumption.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oocitos / Xenopus laevis / Genes ras Límite: Animals Idioma: En Revista: Oncogene Asunto de la revista: BIOLOGIA MOLECULAR / NEOPLASIAS Año: 2006 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oocitos / Xenopus laevis / Genes ras Límite: Animals Idioma: En Revista: Oncogene Asunto de la revista: BIOLOGIA MOLECULAR / NEOPLASIAS Año: 2006 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido