Abstract
THE protein kinase MAP kinase, also called MAP2 kinase, is a serine/threonine kinase whose activation and phosphorylation are induced by a variety of mitogens1–6, and which is thought to have a critical role in a network of protein kinases in mitogenic signal transduction1–7. A burst in kinase activation8,9and protein phosphorylation10 may also be important in triggering the dramatic reorganization of the cell during the transition from interphase to mitosis. The interphase–metaphase transition of microtubule arrays is under the control of p34cdc2 kinase11, a central control element in the G2–M transition of the cell cycle12. Here we show that a Xenopus kinase, closely related to the mitogen-activated mammalian MAP kinase, is phosphorylated and activated during M phase of meiotic and mitotic cell cycles, and that the interphase–metaphase transition of microtubule arrays can be induced by the addition of purified Xenopus M phase-activated MAP kinase or mammalian mitogen-activated MAP kinase to interphase extracts in vitro.
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Gotoh, Y., Nishida, E., Matsuda, S. et al. In vitro effects on microtubule dynamics of purified Xenopus M phase-activated MAP kinase. Nature 349, 251–254 (1991). https://doi.org/10.1038/349251a0
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DOI: https://doi.org/10.1038/349251a0
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