Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry.

摘要: Hyperphosphorylated tau is an integral part of the neurofibrillary tangles that form within neuronal cell bodies, and protein kinase II reported to play a role in pathogenesis Alzheimer's disease. Recently, we (cdk5/p20)-phosphorylated human inhibits microtubule assembly, (cdk5/p20) phosphorylation microtubule-associated results dissociation phosphorylated from microtubules tubulin depolymerization. In studies here, combination mass spectrometric techniques was used study recombinant by vitro. The extent determined measuring molecular using spectrometry. Reaction with resulted formation two major species containing either five or six phosphate groups. specific amino acid residues were analyzing tryptic peptides tandem spectrometry via MALDI/TOF post-source decay electrospray Based on these experiments, conclude can phosphorylate at Thr(181), Thr(205), Thr(212), Thr(217), Ser(396) Ser(404).