Protein kinase C phosphorylates tau and induces its functional alterations.
We found that tau, one of the major microtubule-associated proteins, is a good substrate for protein kinase C. The phosphorylation occurred mainly on serine residues and the sites phosphorylated by protein kinase C were largely different from those phosphorylated by cAMP-dependent protein kinase as analyzed by phosphopeptide mapping. The protein kinase C-mediated phosphorylation of tau reduced its abilities to promote tubulin polymerization and to cross-link actin filaments. The reduction in its abilities was in proportion to the number of phosphates incorporated into tau.
D000199:Actins / Q000378:metabolism; D000818:Animals; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D010449:Peptide Mapping; D010766:Phosphorylation; D010768:Phosphoserine / Q000096:biosynthesis; D011493:Protein Kinase C / Q000378:metabolism*; D011817:Rabbits; D014404:Tubulin / Q000378:metabolism; D016875:tau Proteins
D000199:Actins; D008869:Microtubule-Associated Proteins; D014404:Tubulin; D016875:tau Proteins; D010768:Phosphoserine; D011493:Protein Kinase C