Protein kinase C phosphorylates a 47 Mr protein (F1) directly related to synaptic plasticity.
Ca2+-phospholipid-dependent protein kinase C, and activators of protein kinase C (phosphatidylserine, phorbol esters) stimulate the in vitro phosphorylation of a 47 kdalton phosphoprotein (protein F1) previously shown (Routtenberg, Lovinger and Steward, Behav. neural Biol., 43 (1985) 3-11) to be directly related to the plasticity of long-term potentiation. These data indicate that protein F1 serves as a protein kinase C substrate, and suggest the hypothesis that protein kinase C is involved in processes of long-term potentiation.
Akers
R F
RF
Routtenberg
A
A
D000818:Animals; D002540:Cerebral Cortex / Q000378:metabolism*; D019922:GAP-43 Protein; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009473:Neuronal Plasticity; D010718:Phosphatidylserines / Q000494:pharmacology; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D013570:Synaptic Membranes / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D019922:GAP-43 Protein; D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D010718:Phosphatidylserines; D010750:Phosphoproteins; D011494:Protein Kinases; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate