Protein Kinase C Isoforms Differentially Phosphorylate Human Choline Acetyltransferase Regulating Its Catalytic Activity

Choline acetyltransferase (ChAT) synthesizes acetylcholine in cholinergic neurons; regulation of its activity or response to physiological stimuli is poorly understood. We show that ChAT is differentially phosphorylated by protein kinase C (PKC) isoforms on four serines (Ser-440, Ser-346, Ser-347, a...

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Veröffentlicht in:	The Journal of biological chemistry 2004-12, Vol.279 (50), p.52059-52068
Hauptverfasser:	Tomas Dobransky, Amanda Doherty-Kirby, Ae-Ri Kim, Dyanne Brewer, Gilles Lajoie, Rebecca J. Rylett
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites - genetics Catalytic Domain - genetics Cell Line Choline O-Acetyltransferase - chemistry Choline O-Acetyltransferase - genetics Choline O-Acetyltransferase - metabolism Enzyme Activation Humans In Vitro Techniques Isoenzymes - metabolism Mutagenesis, Site-Directed Myasthenic Syndromes, Congenital - enzymology Myasthenic Syndromes, Congenital - genetics Neurons - enzymology Phosphorylation Protein Kinase C - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Serine - chemistry Spectrometry, Mass, Electrospray Ionization Threonine - chemistry
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