Protein tyrosine kinase signaling in the mouse oocyte cortex during spermegg interactions and anaphase resumption
Protein tyrosine kinase signaling in the mouse oocyte cortex during spermegg interactions and anaphase resumption
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DOI:
10.1002/mrd.22160
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发表时间:
2013-04-01
影响因子:
2.5
通讯作者:
Kinsey, William H.
中科院分区:
文献类型:
--
作者:
McGinnis, Lynda K.;Luo, Jinping;Kinsey, William H.
Fertilization triggers activation of a series of pre-programmed signal transduction pathways in the oocyte that establish a block to polyspermy, induce meiotic resumption, and initiate zygotic development. Fusion between sperm and oocyte results in rapid changes in oocyte intracellular free-calcium levels, which in turn activate multiple protein kinase cascades in the ooplasm. The present study examined the possibility that spermoocyte interaction involves localized activation of oocyte protein tyrosine kinases, which could provide an alternative signaling mechanism to that triggered by the fertilizing sperm. Confocal immunofluorescence analysis with antibodies to phosphotyrosine and phosphorylated protein tyrosine kinases allowed detection of minute signaling events localized to the site of spermoocyte interaction that were not amenable to biochemical analysis. The results provide evidence for localized accumulation of phosphotyrosine at the site of sperm contact, binding, or fusion, which suggests active protein tyrosine kinase signaling prior to and during sperm incorporation. The PYK2 kinase was found to be concentrated and activated at the site of spermoocyte interaction, and likely participates in this response. Widespread activation of PYK2 and FAK kinases was subsequently observed within the oocyte cortex, indicating that sperm incorporation is followed by more global signaling via these kinases during meiotic resumption. The results demonstrate an alternate signaling pathway triggered in mammalian oocytes by sperm contact, binding, or fusion with the oocyte. Mol. Reprod. Dev. 80: 260272, 2013. (c) 2013 Wiley Periodicals, Inc.