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

45 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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@article{220696bab07940879137b017dcb07b4a,

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.",

keywords = "NF-L, Neurofilament, Phosphorylation, Rho-associated kinase",

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

note = "Funding Information: This work was supported in part by Grants-in-Aid for Scienti{\textregistered}c Research and Cancer Research from the Ministry of Education, Science, Sports, and Culture of Japan, special coordination funds from the Science and Technology Agency of the Government of Japan, and Japan Society of the Promotion of Science Research for the Future.",

year = "1998",

month = apr,

day = "17",

doi = "10.1006/bbrc.1998.8446",

language = "English",

volume = "245",

pages = "407--411",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "2",

}

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

N1 - Funding Information: This work was supported in part by Grants-in-Aid for Scienti®c Research and Cancer Research from the Ministry of Education, Science, Sports, and Culture of Japan, special coordination funds from the Science and Technology Agency of the Government of Japan, and Japan Society of the Promotion of Science Research for the Future.

PY - 1998/4/17

Y1 - 1998/4/17

N2 - 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.

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.

KW - NF-L

KW - Neurofilament

KW - Phosphorylation

KW - Rho-associated kinase

UR - https://www.scopus.com/pages/publications/0032540127

UR - https://www.scopus.com/pages/publications/0032540127#tab=citedBy

U2 - 10.1006/bbrc.1998.8446

DO - 10.1006/bbrc.1998.8446

M3 - Article

C2 - 9571164

AN - SCOPUS:0032540127

SN - 0006-291X

VL - 245

SP - 407

EP - 411

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

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

Abstract

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