Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells.

@article{Ebneth1999PhosphorylationOM,
  title={Phosphorylation of MAP2c and MAP4 by MARK kinases leads to the destabilization of microtubules in cells.},
  author={A. Ebneth and G. Drewes and E. Mandelkow},
  journal={Cell motility and the cytoskeleton},
  year={1999},
  volume={44 3},
  pages={
          209-24
        }
}
  • A. Ebneth, G. Drewes, +1 author E. Mandelkow
  • Published 1999
  • Medicine, Biology
  • Cell motility and the cytoskeleton
  • Microtubules serve as transport tracks in molecular mechanisms governing cellular shape and polarity. Rapid transitions between stable and dynamic microtubules are regulated by several factors, including microtubule-associated proteins (MAPs). We have shown that MAP/microtubule affinity regulating kinases (MARK) can phosphorylate the microtubule-associated-proteins MAP4, MAP2c, and tau on their microtubule-binding domain in vitro. This leads to their detachment from microtubules (MT) and an… CONTINUE READING

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