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Publication : Synthesis and function of Mos: the control switch of vertebrate oocyte meiosis.

First Author  Gebauer F Year  1997
Journal  Bioessays Volume  19
Issue  1 Pages  23-8
PubMed ID  9008414 Mgi Jnum  J:39486
Mgi Id  MGI:86880 Doi  10.1002/bies.950190106
Citation  Gebauer F, et al. (1997) Synthesis and function of Mos: the control switch of vertebrate oocyte meiosis. Bioessays 19(1):23-8
abstractText  One distinguishing feature of vertebrate oocyte meiosis is its discontinuity; oocytes are released from their prophase I arrest, usually by hormonal stimulation, only to again halt at metaphase II, where they await fertilization. The product of the c-mos proto-oncogene, Mos, is a key regulator of this maturation process. Mos is a serine-threonine kinase that activates and/or stabilizes maturation-promoting factor (MPF), the master cell cycle switch, through a pathway that involves the mitogen-activated protein kinase (MAPK) cascade. Oocytes arrested at prophase I lack detectable levels of Mos, which must be synthesized from a pool of maternal mRNAs for proper maturation. While Mos is necessary throughout maturation in Xenopus, it seems to be required only for meiosis II in the mouse. The translational activation of c-mos mRNA at specific times during meiosis requires cytoplasmic polyadenylation. Cis- and trans-acting factors for polyadenylation are, therefore, essential elements of maturation.
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