Membrane Clustering and Bungarotoxin Binding by the Nicotinic Acetylcholine Receptor: Role of the β Subunit
Article first published online: 23 NOV 2002
Journal of Neurochemistry
Volume 63, Issue 5, pages 1891–1899, November 1994
How to Cite
Wheeler, S. V., Jane, S. D., Cross, K. M. L., Chad, J. E. and Foreman, R. C. (1994), Membrane Clustering and Bungarotoxin Binding by the Nicotinic Acetylcholine Receptor: Role of the β Subunit. Journal of Neurochemistry, 63: 1891–1899. doi: 10.1046/j.1471-4159.1994.63051891.x
- Issue published online: 23 NOV 2002
- Article first published online: 23 NOV 2002
- Received December 22, 1993; revised manuscript received March 3, 1994; accepted March 8, 1994.
- β subunit;
- Receptor clustering;
- Xenopus oocytes;
- 43-kDa protein
Abstract: Nicotinic acetylcholine receptors (nAChRs) are localised at morphologically distinct regions of the postsynaptic membrane by interactions between the receptor subunits and cytoskeletal proteins, such as the 43-kDa protein. We have used Xenopus oocytes to examine the localisation and pharmacological properties of muscle nAChRs associated with 43-kDa protein and to compare them with hybrid muscle nAChRs containing a β subunit derived from a neuronal source. Receptors expressed on the oocyte outer membrane were visualised using confocal scanning laser microscopy. Coexpression of mouse muscle subunit α1β1γδ and 43-kDa protein transcripts produced discrete receptor aggregates with a diameter of 1–5 µm whose function was partially blocked by application of neuronal bungarotoxin (NBT) at 100 nM. Substitution of the β1 subunit by the neuronal β2 protein produced a functioning receptor that did not aggregate in the presence of 43-kDa protein and was substantially blocked by the same concentration of NBT. Hybrid α1β4γδ receptors exhibited a combination of characteristics in that they clustered like normal muscle subunits in the presence of 43-kDa protein, but showed a sensitivity to NBT intermediate between that of muscle receptors and that of hybrids containing β2. These results suggest that the β subunit is an important determinant in receptor localisation and sensitivity to NBT.