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• W1552162331 endingPage "3521" @default.
• W1552162331 startingPage "3511" @default.
• W1552162331 abstract "The p25rum1 is an inhibitor of Cdc2 kinase expressed in fission yeast and plays an important role in cell-cycle control. As its amino-acid sequence suggests that p25rum1 has putative phosphorylation sites for mitogen-activated protein kinase (MAPK), we investigated the ability of MAPK to phosphorylate p25rum1. Direct in vitro kinase assay using GST-fusion proteins of wild-type as well as various mutants of p25rum1 demonstrated that MAPK phosphorylates the N-terminal portion of p25rum1 and residues Thr13 and Ser19 are major phosphorylation sites for MAPK. In addition, phosphorylation of p25rum1 by MAPK revealed markedly reduced Cdc2 kinase inhibitor ability of the protein. Together with the fact that replacement of both Thr13 and Ser19 with Glu, which mimics the phosphorylated state of these residues, also significantly reduces the activity of p25rum1 as a Cdc2 inhibitor, it was suggested that the phosphorylation of Thr13 and Ser19 negatively regulates the function of p25rum1. Further evidence indicates that phosphorylation of Thr13 and Ser19 may retain a negative effect on the function of p25rum1 even in vivo. Therefore, MAPK may regulate the function of p25rum1 via phosphorylation of its Thr and Ser residues and thus participate in cell cycle control in fission yeast." @default.
• W1552162331 created "2016-06-24" @default.
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• W1552162331 date "2002-07-01" @default.
• W1552162331 modified "2023-10-03" @default.
• W1552162331 title "Rum1, an inhibitor of cyclin-dependent kinase in fission yeast, is negatively regulated by mitogen-activated protein kinase-mediated phosphorylation at Ser and Thr residues" @default.
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• W1552162331 doi "https://doi.org/10.1046/j.1432-1033.2002.03033.x" @default.
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