Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H

FEBS Letters

Weber, Klaus¹  Geisler, Norbert¹  Vandekerckhove, Joel² 

[1] >Max Planck Institute for Biophysical Chemistry, 3400 Göttingen, FRG;Rijksuniversiteit Gent, Laboratory of Genetics, B-9000 Gent, Belgium

关键词: Axon;    Cytoskeleton;    Intermediate filament;    Neurofilament;    Protein kinase;    Serine phosphate;   

DOI  :  10.1016/0014-5793(87)80964-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Diagonal fingerprinting allows the specific purification of those tryptic peptides which change electrophoretic mobility due to a dephosphorylation step introduced after the first dimension. Nine tryptic peptides from the tail domain of porcine neurofilament M protein identify a minimum of 6 phosphorylated serines. Unexpectedly, four of the nine peptides characterize a region of degenerate repetitive sequences. Results on neurofilament H tail, although less complete, yield longer sequences of degenerate repetitive character. Here, all serines present appear to be contained in a lysine-serine-proline unit. This motif also occurs in some but not all M peptides. We suggest that degenerate repetitive sequences in neurofilament M and H tails have a high species-specific drift.

【 授权许可】

Unknown