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

doi:10.1006/bbrc.1998.8446

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 journal › Article

40 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	407-411
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	245
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1998.8446
Publication status	Published - 17-04-1998
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.1998.8446

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Hashimoto, R., Nakamura, Y., Goto, H., Wada, Y., Sakoda, S., Kaibuchi, K., Inagaki, M., & Takeda, M. (1998). Domain- and site-specific phosphorylation of bovine NF-L by Rho-associated kinase. Biochemical and Biophysical Research Communications, 245(2), 407-411. https://doi.org/10.1006/bbrc.1998.8446

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abstract = "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.",

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AU - Hashimoto, Ryota

AU - Nakamura, Yu

AU - Goto, Hidemasa

AU - Wada, Yoshinao

AU - Sakoda, Saburo

AU - Kaibuchi, Kozo

AU - Inagaki, Masaki

AU - Takeda, Masatoshi

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AB - 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.

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