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Journal of Cell Science, Vol 111, Issue 12 1751-1757, Copyright © 1998 by Company of Biologists
JOURNAL ARTICLES |
A Abrieu, T Brassac, S Galas, D Fisher, JC Labbe and M Doree
Centre de Recherches de Biochimie Macromoleculaire, CNRSUPR 1086, 34293 Montpellier cedex 5, France.
We have investigated whether Plx1, a kinase recently shown to phosphorylate cdc25c in vitro, is required for activation of cdc25c at the G2/M-phase transition of the cell cycle in Xenopus. Using immunodepletion or the mere addition of an antibody against the C terminus of Plx1, which suppressed its activation (not its activity) at G2/M, we show that Plx1 activity is required for activation of cyclin B-cdc2 kinase in both interphase egg extracts receiving recombinant cyclin B, and cycling extracts that spontaneously oscillate between interphase and mitosis. Furthermore, a positive feedback loop allows cyclin B-cdc2 kinase to activate Plx1 at the G2/M-phase transition. In contrast, activation of cyclin A-cdc2 kinase does not require Plx1 activity, and cyclin A-cdc2 kinase fails to activate Plx1 and its consequence, cdc25c activation in cycling extracts.
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