Stimulation of tubulin polymerization by MAP-2. Control by protein kinase C-mediated phosphorylation at specific sites in the microtubule-binding region.

@article{Ainsztein1994StimulationOT,
  title={Stimulation of tubulin polymerization by MAP-2. Control by protein kinase C-mediated phosphorylation at specific sites in the microtubule-binding region.},
  author={Alexandra M. Ainsztein and Daniel Lee Purich},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 45},
  pages={28465-71}
}
Microtubule-associated protein-2 (MAP-2) is extensively phosphorylated on serine and threonine residues, and such modifications affect various cellular processes, including microtubule dynamics. Although MAP-2 phosphorylation has been studied both in vitro and in vivo, nothing is known about the exact location of phosphorylated sites influencing the strength of MAP-2 binding to microtubules. Because the microtubule-binding region (MTBR) retains virtually all of the binding affinity of intact… CONTINUE READING

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