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 › peer-review

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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title = "Domain- and site-specific phosphorylation of bovine NF-L by Rho-associated kinase",

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.",

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

year = "1998",

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doi = "10.1006/bbrc.1998.8446",

language = "English",

volume = "245",

pages = "407--411",

journal = "Biochemical and Biophysical Research Communications",

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Domain- and site-specific phosphorylation of bovine NF-L by Rho-associated kinase. / Hashimoto, Ryota; Nakamura, Yu; Goto, Hidemasa; Wada, Yoshinao; Sakoda, Saburo; Kaibuchi, Kozo; Inagaki, Masaki; Takeda, Masatoshi.

In: Biochemical and Biophysical Research Communications, Vol. 245, No. 2, 17.04.1998, p. 407-411.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Domain- and site-specific phosphorylation of bovine NF-L by Rho-associated kinase

AU - Hashimoto, Ryota

AU - Nakamura, Yu

AU - Goto, Hidemasa

AU - Wada, Yoshinao

AU - Sakoda, Saburo

AU - Kaibuchi, Kozo

AU - Inagaki, Masaki

AU - Takeda, Masatoshi

PY - 1998/4/17

Y1 - 1998/4/17

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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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