High molecular weight tau distribution and microtubule stability in neuroblastoma N115 cells.

The localization of high molecular weight (HMW) tau proteins in neuroblastoma N115 cells and of their transcripts was compared to that of non-tyrosinated and tyrosinated tubulin before and after treatment with depolymerizing drugs. Microtubules stained by tau antibodies were present both in a limited region of the cell center and in the cell processes, whereas tau transcripts were detected only in the cell body. The microtubules localized in the cell center and labeled by tau antibodies resisted colcemid treatment, whereas those in the neurites were completely depolymerized by the drug. Microtubules containing stable and unstable microtubule tracts were identified in the neurites after colcemid treatment. These composite microtubules were not labeled by tau antibodies. It is concluded that stable and unstable polymers--localized in the cell center and in the neurites, respectively--contain HMW tau proteins, whereas composite microtubules displayed in the cell processes do not. Microtubule stability in this cell line does not therefore seem to be related to the association of tau proteins to the polymers but, rather, to posttranslational modifications of the tubulin subunits.