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In cells treated with 10 nM okadaic acid (OA), a PP\u20102A\/PP\u20101 inhibitor, the PP\u20101 and \u20102A activities decreased by 60% and 100% respectively and the activities of MAPKs, cdc2 kinase and cdk5, but not of GSK\u20103, increased. OA increased the phosphorylation of \u03c4 at Thr\u2010231\/Ser\u2010235 and Ser\u2010396\/404, but not at Ser\u2010262\/356 or Ser\u2010199\/202. An increase in tyrosinated\/detyrosinated tubulin ratio, a decrease in the microtubule binding activities of \u03c4, MAP1b and MAP2, and cell death were observed. Treatment with 1 \u03bcm taxol partially inhibited the cell death. These data suggest (1) that OA induced hyperphosphorylation of \u03c4 is probably the result of activated MAPK and cdks in addition to decreased PP\u20102A and PP\u20101 activities and (2) that in SY5Y cells the OA induced cell death is associated with a decrease in stable microtubules.<\/jats:p>","DOI":"10.1016\/s0014-5793(98)00346-9","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T17:53:27Z","timestamp":1027619607000},"page":"248-254","source":"Crossref","is-referenced-by-count":101,"title":["The regulation of phosphorylation of \u03c4 in SY5Y neuroblastoma cells: the role of protein 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