Choline acetyltransferase (also designated choactase, choline O-acetyltransferase) synthesizes acetylcholine in cholinergic neurons. Multiple choactase mRNAs with different 5'-noncoding regions are expressed as R-, N1, N2-, S- and M-types. N1-, N2- and R-type mRNAs produce a single short enzyme, while M-type mRNA produces both long and short enzymes. The long enzyme is targeted to the nuclei of cells, whereas the short protein is found in cytoplasm. A novel NFkB binding site is located within the nerve growth factor-responsive enhancer element that is recognized by the NFkB protein p49, but not p65 or p50. Decreased choactase expression and increased NFkB activity are associated with aging and Alzheimer's disease, indicating that p49 is a negative regulator of choactase expression and suggesting a possible mechanism for aging-associated declines in cholinergic function. Phosphorylation of choactase has been shown to enhance choactase catalytic activity. Specifically, Serine 440 is found to be the phosphorylation site in a recombinant human short choactase by protein kinase C and is involved in regulation of the enzyme catalytic activity and binding to subcellular membranes.

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