Domain- and site-specific phosphorylation of bovine NF-L by Rho-associated kinase

Ryota Hashimoto, Yu Nakamura, Hidemasa Goto, Yoshinao Wada, Saburo Sakoda, Kozo Kaibuchi, Masaki Inagaki, Masatoshi Takeda

Research output: Contribution to journalArticlepeer-review

43 Citations (Scopus)


Rho-associated kinase (Rho-kinase), the putative target of the small GTP-binding protein Rho, phosphorylated neurofilament protein (NF-L) in vitro with approximately 1 mole phosphate per mole NF-L. Phosphorylated NF-L no longer formed the 10 nm filaments, and NF-L filaments were phosphorylated with a result of nearly complete disassembly. NF-L phosphorylated by Rho-kinase was digested with trypsin, and digested fragments were assigned by MALDI/TOF. Unique phosphorylation sites were found at Ser-26 and Ser-57 in the head domain of NF-L. These results indicate that domain- and site-specific phosphorylation by Rho-kinase may regulate the assembly-disassembly of NF-L filaments.

Original languageEnglish
Pages (from-to)407-411
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 17-04-1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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