Dephosphorylation of microtubule-binding sites at the neurofilament-H tail domain by alkaline, acid, and protein phosphatases.

@article{Hisanaga1993DephosphorylationOM,
  title={Dephosphorylation of microtubule-binding sites at the neurofilament-H tail domain by alkaline, acid, and protein phosphatases.},
  author={Shin-ichi Hisanaga and S Yasugawa and Tamio Yamakawa and Eishichi Miyamoto and Mitsuo Ikebe and Minaho Uchiyama and Toshihiko Kishimoto},
  journal={Journal of biochemistry},
  year={1993},
  volume={113 6},
  pages={705-9}
}
The dephosphorylation-induced interaction of neurofilaments (NFs) with microtubules (MTs) was investigated by using several phosphatases. Escherichia coli alkaline and wheat germ acid phosphatases increased the electrophoretic mobility of NF-H and NF-M by dephosphorylation, and induced the binding of NF-H to MTs. The binding of NFs to MTs was observed only after the electrophoretic mobility of NF-H approached the exhaustively dephosphorylated level when alkaline phosphatase was used. The number… CONTINUE READING
13 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

Similar Papers

Loading similar papers…