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={Andreas Ebneth and Gunnar Drewes and Eckhard Mandelkow},
  journal={Cell motility and the cytoskeleton},
  year={1999},
  volume={44 3},
  pages={209-24}
}
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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