Phosphorylation of 68 kDa neurofilament proteins has no significant effect on their assembly.
Native low molecular weight neurofilaments (NF-L) from bovine spinal cord with original phosphate content of 0.4 moles of phosphate per 1 mol of protein were phosphorylated with cyclic AMP dependent protein kinase and protein kinase C. In a similar way recombinant mouse NF-L proteins which did not contain any phosphate were phosphorylated with the same enzymes in both, the assembled and disassembled forms. The final phosphate content in both types of NF-L proteins reached about 4 moles of phosphate per 1 mol of protein. This phosphorylation had no effect on the assembly of NF-L into filaments as observed by electron microscopy.
Sonská
A
A
Department of Biochemistry, Charles University, Prague, Czech Republic.
Entlicher
G
G
D000818:Animals; D002417:Cattle; D051379:Mice; D008854:Microscopy, Electron; D016900:Neurofilament Proteins / Q000032:analysis* / Q000378:metabolism* / Q000648:ultrastructure; D010766:Phosphorylation; D011994:Recombinant Proteins / Q000378:metabolism / Q000648:ultrastructure; D013116:Spinal Cord / Q000737:chemistry*
D016900:Neurofilament Proteins; D011994:Recombinant Proteins; C044882:neurofilament protein L