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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cattle
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Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
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Intracellular Signaling Peptides and Proteins
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Kinetics
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Microscopy, Electron
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / ultrastructure
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Neurofilament Proteins / chemistry*
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Neurofilament Proteins / ultrastructure
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Peptide Fragments / chemistry
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Phosphates / metabolism
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Phosphorylation
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Protein Serine-Threonine Kinases / metabolism*
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Sequence Alignment
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Sequence Analysis
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Trypsin / metabolism
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rho-Associated Kinases
Substances
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Intracellular Signaling Peptides and Proteins
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Nerve Tissue Proteins
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Neurofilament Proteins
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Peptide Fragments
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Phosphates
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neurofilament protein L
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Guanosine 5'-O-(3-Thiotriphosphate)
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Protein Serine-Threonine Kinases
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rho-Associated Kinases
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Trypsin