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The Journal of Neuroscience, November 17, 2004, 24(46):10502-10510; doi:10.1523/JNEUROSCI.3315-04.2004
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Cellular/Molecular
The Role of Palmitoylation in Functional Expression of Nicotinic  7 Receptors
Renaldo C. Drisdel,
Ehrine Manzana, and
William N. Green
Department of Neurobiology, Pharmacology, and Physiology, University of Chicago, Chicago, Illinois 60637
Neuronal  -bungarotoxin receptors (BgtRs) are nicotinic receptors that require as yet unidentified post-translational modifications to achieve functional expression. In this study, we examined the role of protein palmitoylation in BgtR expression. BgtR 7 subunits are highly palmitoylated in neurons from brain and other cells capable of BgtR expression, such as pheochromocytoma 12 (PC12) cells. In PC12 cells, 7 subunits are palmitoylated with a stoichiometry of approximately one palmitate per subunit, and inhibition of palmitoylation blocks BgtR expression. In cells incapable of BgtR expression, such as human embryonic kidney cells, 7 subunits are not significantly palmitoylated. However, in these same cells, chimeric subunits with the N-terminal half of 7 fused to the C-terminal half of serotonin-3A receptor (7/5-HT3A) subunits form functional BgtRs that are palmitoylated to an extent similar to that of BgtR7 subunits in PC12 cells. Palmitoylation of PC12 and 7/5-HT3A BgtRs occurred during assembly in the endoplasmic reticulum (ER). In conclusion, our data indicate a function for protein palmitoylation in which palmitoylation of assembling 7 subunits in the ER has a role in the formation of functional BgtRs.
Key words: acetylcholine (ACh); bungarotoxin; nicotinic; palmitate; pheochromocytoma (PC12, PC-12); neuronal
Received Sep 12, 2003;
revised October 1, 2004;
accepted October 5, 2004.
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