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Domain- and Site-Specific Phosphorylation of Bovine NF-L by Rho-Associated Kinase

Domain- and Site-Specific Phosphorylation of Bovine NF-L by Rho-Associated Kinase

Authors :
Hidemasa Goto
Yoshinao Wada
Masaki Inagaki
Ryota Hashimoto
Yu Nakamura
Saburo Sakoda
Masatoshi Takeda
Kozo Kaibuchi
Source :
Biochemical and Biophysical Research Communications. 245:407-411
Publication Year :
1998
Publisher :
Elsevier BV, 1998.

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.

Details

ISSN :
0006291X
Volume :
245
Database :
OpenAIRE
Journal :
Biochemical and Biophysical Research Communications
Accession number :
edsair.doi.dedup.....b7c471e84b9751a1b72fd0402c515a48
Full Text :
https://doi.org/10.1006/bbrc.1998.8446