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

Bioessays. 1997 Jan;19(1):23-8. doi: 10.1002/bies.950190106.


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.

Publication types

  • Review

MeSH terms

  • Animals
  • Base Sequence
  • Calcium-Calmodulin-Dependent Protein Kinases / physiology
  • Female
  • Meiosis / physiology*
  • Mice
  • Oocytes / cytology
  • Oocytes / growth & development
  • Oocytes / physiology*
  • Oogenesis / physiology
  • Protein Biosynthesis
  • Proto-Oncogene Proteins c-mos / genetics
  • Proto-Oncogene Proteins c-mos / physiology*
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Xenopus


  • RNA, Messenger
  • Proto-Oncogene Proteins c-mos
  • Calcium-Calmodulin-Dependent Protein Kinases