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Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation

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Abstract

We have cloned a mousewee1 kinase cDNA (mwee1). The clone is 2258 bp in length and its open reading frame corresponds to 646 amino acid residues. The molecular weight of this kinase is 87 kDa in SDS-PAGE, which is about 1.7-fold larger than the human p50wee1 kinase reported previously. In a cell cycle, the mousewee1 kinase is phosphorylated at M-phase, and anin vitro study using a mitotic extract revealed that phosphorylation occurs in the N-terminal domain, which is absent from the humanwee1 kinase, resulting in inactivation of the kinase activity. The N-terminal domain or entire molecule is extensively phosphorylated bycdc2-cyclin B kinase. Furthermore, the activity of thewee1 kinase was reduced by phosphorylation with the mitotic extract which containedcdc2-cyclin B kinase

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Honda, R., Tanaka, H., Ohba, Y. et al. Mouse p87wee1 kinase is regulated by M-phase specific phosphorylation. Chromosome Res 3, 300–308 (1995). https://doi.org/10.1007/BF00713068

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  • DOI: https://doi.org/10.1007/BF00713068

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