Multisite phosphorylation of tau proteins from rat brain.
tau proteins from adult and young rat brains were phosphorylated in vitro by protein kinases present in microtubule preparations. Several phosphates were incorporated in each molecular species of this group of proteins. Cyclic AMP dependent protein kinases and casein kinase (type I) phosphorylated tau proteins on different sites. These observations indicate that tau proteins are an example of multisite phosphorylation.
D000255:Adenosine Triphosphate; D000818:Animals; D001921:Brain / Q000378:metabolism*; D047388:Casein Kinases; D007700:Kinetics; D008870:Microtubules / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats; D016875:tau Proteins
D009419:Nerve Tissue Proteins; D010446:Peptide Fragments; D010761:Phosphorus Radioisotopes; D011506:Proteins; D016875:tau Proteins; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D047388:Casein Kinases