Phosphorylation of neurofilament H subunit at the tail domain by CDC2 kinase dissociates the association to microtubules.

摘要: We sought the mammalian neurofilament tail domain-specific kinase. Several well known kinases including cAMP-dependent protein kinase, kinase C, Ca(2+)-calmodulin-dependent II, casein I, and II phosphorylated high (NF-H) middle molecular mass subunit (NF-M) of bovine neurofilaments, but they did not reduced electrophoretic mobility dephosphorylated form NF-M NF-H by phosphorylation nor was amount increased dephosphorylation NF proteins, indicating that sites these are major in vivo at domain. In contrast, cdc2 specifically NF-H. 4 mol phosphates were incorporated per this returned to position isolated, fully Furthermore, dissociated binding microtubules. Phosphorylation located carboxyl-terminal The KSPXK motif, KSPXX, repetitive sequence suggested be site using synthetic peptides.