The Journal of Cell Biology, Vol 115, 337-344, Copyright © 1991 by The Rockefeller University Press

ARTICLES

Okadaic acid mimics a nuclear component required for cyclin B-cdc2 kinase microinjection to drive starfish oocytes into M phase

A Picard, JC Labbe, H Barakat, JC Cavadore and M Doree
Laboratoire Arago, Banyuls, France.

G2-arrested oocytes contain cdc2 kinase as an inactive cyclin B-cdc2 complex. When a small amount of highly purified and active cdc2 kinase, prepared from starfish oocytes at first meiotic metaphase, is microinjected into Xenopus oocytes, it induces activation of the inactive endogenous complex and, as a consequence, drives the recipient oocytes into M phase. In contrast, the microinjected kinase undergoes rapid inactivation in starfish oocytes, which remain arrested at G2. Endogenous cdc2 kinase becomes activated in both nucleated and enucleated starfish oocytes injected with cytoplasm taken from maturing oocytes at the time of nuclear envelope breakdown, but only cytoplasm taken from nucleated oocytes becomes able thereafter to release second recipient oocytes from G2 arrest, and thus contains M phase-promoting factor (MPF) activity. Both nucleated and enucleated starfish oocytes produce MPF activity when type 2A phosphatase is blocked by okadaic acid. If type 2A phosphatase is only partially inhibited, neither nucleated nor enucleated oocytes produce MPF activity, although both do so if purified cdc2 kinase is subsequently injected as a primer to activate the endogenous kinase. The nucleus of starfish oocytes contains an inhibitor of type 2A phosphatase, but neither active nor inactive cdc2 kinase. Microinjection of the content of a nucleus into the cytoplasm of G2-arrested starfish oocytes activates endogenous cdc2 kinase, produces MPF activity, and drives the recipient oocytes into M phase. Together, these results show that the MPF amplification loop is controlled, both positively and negatively, by cdc2 kinase and type 2A phosphatase, respectively. Activation of the MPF amplification loop in starfish requires a nuclear component to inhibit type 2A phosphatase in cytoplasm.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Facebook    Reddit    Technorati    Twitter    What's this?

This article has been cited by other articles:

• Sugiura, K., Naito, K., Endo, T., Tojo, H. (2006). Study of Germinal Vesicle Requirement for the Normal Kinetics of Maturation/M-Phase-Promoting Factor Activity During Porcine Oocyte Maturation. Biol. Reprod. 74: 593-600 [Abstract] [Full Text]  
• Doree, M., Hunt, T. (2002). From Cdc2 to Cdk1: when did the cell cycle kinase join its cyclin partner?. J. Cell Sci. 115: 2461-2464 [Abstract] [Full Text]  
• Peter, M., Labbe, J.-C., Doree, M., Mandart, E. (2002). A new role for Mos in Xenopus oocyte maturation: targeting Myt1 independently of MAPK. Development 129: 2129-2139 [Abstract] [Full Text]  
• Abrieu, A, Doree, M, Fisher, D (2001). The interplay between cyclin-B-Cdc2 kinase (MPF) and MAP kinase during maturation of oocytes. J. Cell Sci. 114: 257-267 [Abstract]  
• Bastians, H., Topper, L. M., Gorbsky, G. L., Ruderman, J. V. (1999). Cell Cycle-regulated Proteolysis of Mitotic Target Proteins. Mol. Biol. Cell 10: 3927-3941 [Abstract] [Full Text]  
• Patra, D., Dunphy, W. G. (1998). Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- promoting complex at mitosis. Genes Dev. 12: 2549-2559 [Abstract] [Full Text]  
• Thompson, L. J., Fields, A. P. (1996). beta II Protein Kinase C Is Required for the G2/M Phase Transition of Cell Cycle. J. Biol. Chem. 271: 15045-15053 [Abstract] [Full Text]  
• Patra, D, Dunphy, W G (1996). Xe-p9, a Xenopus Suc1/Cks homolog, has multiple essential roles in cell cycle control.. Genes Dev. 10: 1503-1515 [Abstract]  
• Geneviere-Garrigues, A., Barakat, A, Doree, M, Moreau, J., Picard, A (1995). Active cyclin B-cdc2 kinase does not inhibit DNA replication and cannot drive prematurely fertilized sea urchin eggs into mitosis. J. Cell Sci. 108: 2693-2703 [Abstract]  
• Mayer-Jaekel, R., Ohkura, H, Ferrigno, P, Andjelkovic, N, Shiomi, K, Uemura, T, Glover, D., Hemmings, B. (1994). Drosophila mutants in the 55 kDa regulatory subunit of protein phosphatase 2A show strongly reduced ability to dephosphorylate substrates of p34cdc2. J. Cell Sci. 107: 2609-2616 [Abstract]  
• Paulson, J., Ciesielski, W., Schram, B., Mesner, P. (1994). Okadaic acid induces dephosphorylation of histone H1 in metaphase-arrested HeLa cells. J. Cell Sci. 107: 267-273 [Abstract]  
• Gavin, A., Cavadore, J., Schorderet-Slatkine, S (1994). Histone H1 kinase activity, germinal vesicle breakdown and M phase entry in mouse oocytes. J. Cell Sci. 107: 275-283 [Abstract]  
• Hosoya, N, Mitsui, M, Yazama, F, Ishihara, H, Ozaki, H, Karaki, H, Hartshorne, D., Mohri, H (1993). Changes in the cytoskeletal structure of cultured smooth muscle cells induced by calyculin-A. J. Cell Sci. 105: 883-890 [Abstract]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents