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
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.
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U2 - 10.1006/bbrc.1998.8446
DO - 10.1006/bbrc.1998.8446
M3 - Article
C2 - 9571164
AN - SCOPUS:0032540127
VL - 245
SP - 407
EP - 411
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -