Functional regulation of choline acetyltransferase by phosphorylation.
作者： Tomas Dobransky , R. Jane Rylett
关键词:
摘要: Choline acetyltransferase (ChAT) catalyzes synthesis of acetylcholine (ACh) in cholinergic neurons. ACh is regulated by availability precursors choline and acetyl coenzyme A or activity ChAT; ChAT regulates under some conditions. Posttranslational phosphorylation a common mechanism for regulating the function proteins. Analysis primary sequence 69-kD human indicates that it has putative consensus sequences multiple protein kinases. phosphorylated on serine-440 threonine-456 kinase C CaM II, respectively. These events regulate enzyme, as well its binding to plasma membrane interaction with other cellular It relevant investigate differences constitutive inducible patterns physiological conditions response challenges neurons may be exposed to, determine how changes relate neurochemical transmission.
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EA Clark, KL Leach, JQ Trojanowski, VM Lee, Characterization and differential distribution of the three major human protein kinase C isozymes (PKC alpha, PKC beta, and PKC gamma) of the central nervous system in normal and Alzheimer's disease brains. Laboratory Investigation. ,vol. 64, pp. 35- 44 ,(1991)
R. Jane Rylett, Bonnie M. Schmidt, Regulation of the synthesis of acetylcholine. Progress in Brain Research. ,vol. 98, pp. 161- 166 ,(1993) , 10.1016/S0079-6123(08)62394-8
B. Collier, A. Tandon, M.A.M. Prado, M. Bachoo, Storage and release of acetylcholine in a sympathetic ganglion. Progress in Brain Research. ,vol. 98, pp. 183- 189 ,(1993) , 10.1016/S0079-6123(08)62397-3
T. Yamauchi, H. Nakata, H. Fujisawa, A new activator protein that activates tryptophan 5-monooxygenase and tyrosine 3-monooxygenase in the presence of Ca2+-, calmodulin-dependent protein kinase. Purification and characterization. Journal of Biological Chemistry. ,vol. 256, pp. 5404- 5409 ,(1981) , 10.1016/S0021-9258(19)69215-X
H Misawa, K Ishii, T Deguchi, Gene expression of mouse choline acetyltransferase. Alternative splicing and identification of a highly active promoter region. Journal of Biological Chemistry. ,vol. 267, pp. 20392- 20399 ,(1992) , 10.1016/S0021-9258(19)88714-8
C Cozzari, B K Hartman, Choline acetyltransferase. Purification procedure and factors affecting chromatographic properties and enzyme stability. Journal of Biological Chemistry. ,vol. 258, pp. 10013- 10019 ,(1983) , 10.1016/S0021-9258(17)44599-6
L B Hersh, Kinetic studies of the choline acetyltransferase reaction using isotope exchange at equilibrium. Journal of Biological Chemistry. ,vol. 257, pp. 12820- 12825 ,(1982) , 10.1016/S0021-9258(18)33587-7
Michael B. Yaffe, Lewis C. Cantley, Grabbing phosphoproteins Nature. ,vol. 402, pp. 30- 31 ,(1999) , 10.1038/46925
Isabelle Robert, Christiane Quirin-Stricker, A novel untranslated 'exon H' of the human choline acetyltransferase gene in placenta. Journal of Neurochemistry. ,vol. 79, pp. 9- 16 ,(2008) , 10.1046/J.1471-4159.2001.00508.X
Bonnie M. Schmidt, R. Jane Rylett, Phosphorylation of Rat Brain Choline Acetyltransferase and Its Relationship to Enzyme Activity Journal of Neurochemistry. ,vol. 61, pp. 1774- 1781 ,(1993) , 10.1111/J.1471-4159.1993.TB09815.X