Phosphorylation of elongation factor 2 in the rat superior cervical ganglion.
Elongation factor 2 (EF-2) and its associated kinase, Ca2+/calmodulin-dependent protein kinase III, have recently been identified as a major protein phosphorylation system in mammalian tissues. We have measured the phosphorylation of EF-2 in 32P-labeled superior cervical ganglia. Phosphorylation of EF-2 was increased by preganglionic stimulation or by treatment of the ganglion with dimethylphenylpiperazinium or veratridine. Increases in EF-2 phosphorylation presumably reflect the activation of Ca2+/calmodulin-dependent protein kinase III by nicotinic stimulation and depolarization. The phosphorylation of EF-2 may help to coordinate neuronal protein synthesis with neuronal activity.
Cahill
A L
AL
Department of Pediatrics, University of Chicago, IL 60637.
Applebaum
R
R
Perlman
R L
RL
D000818:Animals; D004558:Electric Stimulation; D005728:Ganglia, Sympathetic / Q000378:metabolism* / Q000502:physiology; D007106:Immune Sera; D007700:Kinetics; D008970:Molecular Weight; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000378:metabolism*; D010750:Phosphoproteins / Q000302:isolation & purification; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats
D007106:Immune Sera; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010750:Phosphoproteins; D011494:Protein Kinases