The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules.

@article{Prez2000TheFM,
  title={The FTDP-17-linked mutation R406W abolishes the interaction of phosphorylated tau with microtubules.},
  author={Mar{\'i}a Teresa Olaya P{\'e}rez and Filip Lim and Montserrat Arrasate and Jes{\'u}s {\'A}vila},
  journal={Journal of neurochemistry},
  year={2000},
  volume={74 6},
  pages={
          2583-9
        }
}
The recent finding that several point mutations in the gene encoding for the microtubule-binding protein tau correlate with neurological disorders has heightened interest in the mechanisms of destabilization of this protein. In this study the functional consequences of the tau mutation R406W on the interaction of the protein with microtubules have been analyzed. Mutated tau is less phosphorylated than its normal counterpart at serines 396 and 404. Furthermore, the phosphorylated mutant protein… CONTINUE READING
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