Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest

Ellen K. Shibuya, Teri G. Boulton, Melanie H. Cobb, Joan V. Ruderman

Research output: Contribution to journalArticle

140 Citations (Scopus)

Abstract

Clam oocytes are arrested naturally at the G2/M border in meiosis and contain an inactive 42 kDa ERK/MAP kinase, p42MAPK. Following fertilization, p42MAPK is rapidly phosphorylated on tyrosine residues and concomitantly activated. Both tyrosine phosphorylation and activation of p42MAPK begin within 2-3 min of fertilization, peak at ∼15 min, then rapidly decline and disappear around the end of meiosis I. Neither the tyrosine phosphorylated form of p42MAPK nor p42MAPK activity reappears during meiosis II or the succeeding mitotic cell cycles. High doses of molybdate, a potent PTPase inhibitor, block the phosphorylation of p42MAPK and entry into the cell cycle. Lower doses of molybdate delay both p42MAPK phosphorylation and the release from cell cycle arrest, but once cells have re-entered the cell cycle, they continue with near-normal timing. These results argue that the transient activation of p42MAPK at fertilization is a one-time event linked to release from cell cycle arrest. In trying to reconcile this one-time activation of p42MAPK in clam embryos with the recurring, M-phase specific activation of MBP/MAP kinases reported in other systems, we show that cdc2 kinase contributes a major portion of the MBP kinase activity in mitotic extracts. Furthermore, a small fraction of p42MAPK and other related kinases are present in p13suc1-bound material, cautioning against the use of p13suc1 beads for experiments where, in addition to cdc2, the unaccounted presence of other kinase activities could be misleading.

Original languageEnglish (US)
Pages (from-to)3963-3975
Number of pages13
JournalEMBO Journal
Volume11
Issue number11
StatePublished - Nov 1992

Fingerprint

Mitogen-Activated Protein Kinase 1
Cell Cycle Checkpoints
Oocytes
Phosphotransferases
Chemical activation
Cells
Phosphorylation
Meiosis
Fertilization
Tyrosine
Cell Cycle
Bivalvia
Protein Tyrosine Phosphatases
Extracellular Signal-Regulated MAP Kinases
Cell Division
Embryonic Structures
Experiments
molybdate

Keywords

  • Cell cycle arrest
  • Clam oocytes
  • Fertilization
  • MAP kinase
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Shibuya, E. K., Boulton, T. G., Cobb, M. H., & Ruderman, J. V. (1992). Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest. EMBO Journal, 11(11), 3963-3975.

Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest. / Shibuya, Ellen K.; Boulton, Teri G.; Cobb, Melanie H.; Ruderman, Joan V.

In: EMBO Journal, Vol. 11, No. 11, 11.1992, p. 3963-3975.

Research output: Contribution to journalArticle

Shibuya, EK, Boulton, TG, Cobb, MH & Ruderman, JV 1992, 'Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest', EMBO Journal, vol. 11, no. 11, pp. 3963-3975.
Shibuya EK, Boulton TG, Cobb MH, Ruderman JV. Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest. EMBO Journal. 1992 Nov;11(11):3963-3975.
Shibuya, Ellen K. ; Boulton, Teri G. ; Cobb, Melanie H. ; Ruderman, Joan V. / Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest. In: EMBO Journal. 1992 ; Vol. 11, No. 11. pp. 3963-3975.
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