Involvement of protein kinase C in the regulation of assembly-disassembly of neurofilaments in vitro.
Protein kinase C phosphorylated the major mammalian neurofilament protein (NF-L) with approximately 3 mol phosphate per mol protein. The phosphorylated NF-L no longer formed the filaments. Sequential analysis of the tryptic phosphopeptides, together with the known primary sequence, revealed that Ser-12, Ser-27, Ser-33 and Ser-51 were phosphorylated by protein kinase C. These findings contribute toward elucidation of mechanisms regulating the functions of neurofilaments.
Gonda
Y
Y
Laboratory of Experimental Radiology, Aichi Cancer Center Research Institute, Nagoya, Japan.
Nishizawa
K
K
Ando
S
S
Kitamura
S
S
Minoura
Y
Y
Nishi
Y
Y
Inagaki
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000378:metabolism; D007381:Intermediate Filament Proteins / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D007382:Intermediate Filaments / Q000648:ultrastructure; D007700:Kinetics; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D016900:Neurofilament Proteins; D010449:Peptide Mapping; D010748:Phosphopeptides / Q000302:isolation & purification; D010766:Phosphorylation; D011487:Protein Conformation; D011493:Protein Kinase C / Q000378:metabolism*; D013552:Swine
D007381:Intermediate Filament Proteins; D016900:Neurofilament Proteins; D010748:Phosphopeptides; D011493:Protein Kinase C