. The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases. FEBS Lett. 1998 Apr 17;426(2):248-54. PubMed.


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  1. It is interesting that these authors report that treatment with okadaic acid (OA) did not alter tau phosphorylation at Ser 262/356, yet microtubule-binding ability of tau was decreased - in contrast to the Mandelkows' suggestion that microtubule binding of tau is heavily dependent
    on Ser 262 phosphorylation state. It is also interesting that although the present authors report that "in SY5Y cells the OA induced cell death is associated with a decrease in stable microtubules" Arendt recently reported in Neurobiology of Aging a decoupling of OA induced tau phosphorylation and apoptotic cell death in vivo, especially in dentate gyrus granule cells. The reasons for differences in results and interpretations require further study.

  2. Phosphorylation is regulated by kinases and phosphatases. SY5Y cells are interesting because of neuronal derivative line and worth examining for kinase activity and phosphorylation. Such results must be useful for the treatment of the drug to control tau phosphorylation.

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