MAP4 is the in vivo substrate for CDC2 kinase in HeLa cells: identification of an M-phase specific and a cell cycle-independent phosphorylation site in MAP4.

@article{Ookata1997MAP4IT,
  title={MAP4 is the in vivo substrate for CDC2 kinase in HeLa cells: identification of an M-phase specific and a cell cycle-independent phosphorylation site in MAP4.},
  author={Kayoko Ookata and Shin-ichi Hisanaga and Mutsumi Sugita and Akira Okuyama and Hiromu Murofushi and Haruki Kitazawa and Sheila Chari and Jeannette Chlo{\"e} Bulinski and Takeo Kishimoto},
  journal={Biochemistry},
  year={1997},
  volume={36 50},
  pages={15873-83}
}
We reported previously that cdc2 kinase decreased the microtubule-stabilizing ability of a major HeLa cell microtubule-associated protein, MAP4, by phosphorylation in vitro [Ookata, K., et al. (1995) J. Cell Biol. 128, 849-862]. An important question raised by this study is whether MAP4 is indeed phosphorylated by cdc2 kinase at mitosis in vivo. We present here evidence that cdc2 kinase is the major M-phase MAP4 kinase, and, further, we identify two phosphorylation sites within the proline-rich… CONTINUE READING

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