NOTES: Meiotic Induction by Xenopus Cyclin B Is Accelerated by Coexpression with mos^Xe

REFERENCES

• Cyert, M. S., and M. W. Kirschner. 1988. Regulation of MPF activity in vitro. Cell 53:185-195.
   PubMed Web of Science ®Google Scholar
• Draetta, G., F. Luca, J. Westendorf, L. Brizuela, J. Ruderman, and D. Beach. 1989. cdc2 protein kinase is complexed with both cyclin A and B: evidence for proteolytic inactivation of MPF. Cell 56:829-838.
   PubMed Web of Science ®Google Scholar
• Draetta, G., H. Piwnica-Worms, D. Morrison, B. Druker, T. Roberts, and D. Beach. 1988. Human cdc2 protein kinase is a major cell cycle-regulated tyrosine kinase substrate. Nature (London) 336:738-744.
   PubMed Web of Science ®Google Scholar
• Dunphy, W. G., L. Brizuela, D. Beach, and J. Newport. 1988. The Xenopus cdc2 protein is a component of MPF, a cytoplasmic regulator of mitosis. Cell 54:423-431.
   PubMed Web of Science ®Google Scholar
• Dunphy, W. G., and J. W. Newport. 1989. Fission yeast pl3 blocks mitotic activation and tyrosine dephosphorylation of the Xenopus cdc2 protein kinase. Cell 58:181-191.
   PubMed Web of Science ®Google Scholar
• Felix, M.-A., P. Cohen, and E. Karsenti. 1990. Cdc2Hl kinase is negatively regulated by a type 2A phosphatase in the Xenopus early embryonic cell cycle: evidence from the effects of okadaic acid. EMBO J. 9:675-683.
   PubMedGoogle Scholar
• Freeman, R. S., J. P. Kanki, S. M. Ballantyne, K. M. Pickham, and D. J. Donoghue. 1990. Effects of the v-mos oncogene on Xenopus development: meiotic induction in oocytes and mitotic arrest in cleaving embryos. J. Cell Biol. 111:533-541.
   PubMedGoogle Scholar
• Freeman, R. S., K. M. Pickham, J. P. Kanki, B. A. Lee, S. V. Pena, and D. J. Donoghue. 1989. Xenopus homolog of the mos protooncogene transforms mammalian fibroblasts and induces maturation of Xenopus oocytes. Proc. Natl. Acad. Sci. USA 86:5805-5809.
   PubMed Web of Science ®Google Scholar
• Gautier, J., T. Matsukawa, P. Nurse, and J. Mailer. 1989. Dephosphorylation and activation of Xenopus p34cdc2 protein kinase during the cell cycle. Nature (London) 339:626-629.
   PubMed Web of Science ®Google Scholar
• Gautier, J., J. Minshull, M. Lohka, M. Glotzer, T. Hunt, and J. L. Maller. 1990. Cyclin is a component of maturation-promoting factor from Xenopus. Cell 60:487-494.
   PubMed Web of Science ®Google Scholar
• Gautier, J., C. Norbury, M. Lohka, P. Nurse, and J. Mailer. 1988. Purified maturation-promoting factor contains the product of a Xenopus homolog of the fission yeast cell cycle control gene cdc2+ Cell 54:433-439.
   PubMed Web of Science ®Google Scholar
• Gerhart, J., M. Wu, and M. Kirschner. 1984. Cell cycle dynamics of an M-phase-specific cytoplasmic factor in Xenopus laevis oocytes and eggs. J. Cell Biol. 98:1247-1255.
   PubMedGoogle Scholar
• Goris, J., J. Hermann, P. Hendrix, R. Ozon, and W. Merlevede. 1989. Okadaic acid, a specific protein phosphatase inhibitor, induces maturation and MPF formation in Xenopus laevis oocytes. FEBS Lett. 245:91-94.
   PubMed Web of Science ®Google Scholar
• Gould, K., and P. Nurse. 1989. Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis. Nature (London) 342:39-45.
   PubMed Web of Science ®Google Scholar
• Labbe, J. C., A. Picard, G. Peaucellier, J. C. Cavadore, P. Nurse, and M. Doree. 1989. Purification of MPF from starfish: identification as the Hl histone kinase p34cdc2 and a possible mechanism for its periodic activation. Cell 57:253-263.
   PubMed Web of Science ®Google Scholar
• Mailer, J., M. Wu, and J. C. Gerhart. 1977. Changes in protein phosphorylation accompanying maturation of xenopus laevis oocytes. Dev. Biol. 58:295-312.
   PubMedGoogle Scholar
• Masui, Y., and C. L. Markert. 1971. Cytoplasmic control of nuclear behavior during meiotic maturation of frog oocytes. J. Exp. Zool. 177:129-146.
   PubMedGoogle Scholar
• Merriam, R. W. 1971. Progesterone-induced maturational events in oocytes of Xenopus laevis. Exp. Cell Res. 68:81-87.
   PubMedGoogle Scholar
• Minshull, J., J. J. Blow, and T. Hunt. 1989. Translation of cyclin mRNA is necessary for extracts of activated Xenopus eggs to enter mitosis. Cell 56:947-956.
   PubMed Web of Science ®Google Scholar
• Morla, A. O., G. Draetta, D. Beach, and J. Y. J. Wang. 1989. Reversible tyrosine phosphorylation of cdc2: dephosphorylation accompanies activation during entry into mitosis. Cell 58:193-203.
   PubMed Web of Science ®Google Scholar
• Murray, A. W., M. J. Solomon, and M. W. Kirschner. 1989. The role of cyclin synthesis and degradation in the control of maturation promoting factor activity. Nature (London) 339:280-286.
   PubMed Web of Science ®Google Scholar
• Nurse, P. 1990. Universal control mechanism regulating onset of M-phase. Nature (London) 344:503-508.
   PubMed Web of Science ®Google Scholar
• Pines, J., and T. Hunt. 1987. Molecular cloning and characterization of the mRNA for cyclin from sea urchin eggs. EMBO J. 6:2987-2995.
   PubMedGoogle Scholar
• Pines, J., and T. Hunter. 1989. Isolation of a human cyclin cDNA: evidence for cyclin mRNA and protein regulation in the cell cycle and for interaction with p34cdc2. Cell 58:833-846.
   PubMed Web of Science ®Google Scholar
• Pondaven, P., L. Meijer, and D. Beach. 1990. Activation of M-phase-specific histone Hl kinase by modification of the phosphorylation of its p34cdc2 and cyclin components. Genes Dev. 4:9-17.
   PubMed Web of Science ®Google Scholar
• Roy, L. M., B. Singh, J. Gautier, R. B. Arlinghaus, S. K. Nordeen, and J. L. Mailer. 1990. The cyclin B2 component of MPF is a substrate for the c-mosxe proto-oncogene product. Cell 61:825-831.
   PubMedGoogle Scholar
• Sagata, N., I. Daar, M. Oskarsson, S. D. Showalter, and G. F. Vande Woude. 1989. The product of the mos proto-oncogene as a candidate “initiator” for oocyte maturation. Science 245:643-646.
   PubMed Web of Science ®Google Scholar
• Sagata, N., M. Oskarsson, T. Copeland, J. Brumbaugh, and G. F. Vande Woude. 1988. Function of c-mos proto-oncogene product in meiotic maturation in Xenopus oocytes. Nature (London) 335:519-525.
   PubMed Web of Science ®Google Scholar
• Sagata, N., N. Watanabe, G. F. Vande Woude, and Y. Ikawa. 1989. The c-mos proto-oncogene product is a cytostatic factor responsible for meiotic arrest in vertebrate eggs. Nature (London) 342:512-518.
   PubMed Web of Science ®Google Scholar
• Swenson, K. I., K. M. Farrell, and J. V. Ruderman. 1986. The clam embryo protein cyclin A induces entry into M phase and the resumption of meiosis in Xenopus oocytes. Cell 47:861-870.
   PubMed Web of Science ®Google Scholar
• Watanabe, N., G. F. Vande Woude, Y. Ikawa, and N. Sagata. 1989. Specific proteolysis of the c-mos proto-oncogene product by calpain on fertilization of Xenopus eggs. Nature (London) 342:505-511.
   PubMed Web of Science ®Google Scholar
• Westendorf, J. M., K. I. Swenson, and J. V. Ruderman. 1989. The role of cyclin B in meiosis I. J. Cell Biol. 108:1431-1444.
   PubMed Web of Science ®Google Scholar