Membrane clustering and bungarotoxin binding by the nicotinic acetylcholine receptor: role of the β subunit


Wheeler, Susan V., Jane, Steven D., Cross, Kathryn M.L., Chad, John E. and Foreman, Richard C. (1994) Membrane clustering and bungarotoxin binding by the nicotinic acetylcholine receptor: role of the β subunit. Journal of Neurochemistry, 63, (5), 1891-1899. (doi:10.1046/j.1471-4159.1994.63051891.x).

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Description/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.

Item Type: Article
ISSNs: 0022-3042 (print)
Related URLs:
Keywords: β subunit, nicotinic, receptor clustering, xenopus oocytes, 43-kDa protein
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56208
Date Deposited: 22 Aug 2008
Last Modified: 27 Mar 2014 18:38
URI: http://eprints.soton.ac.uk/id/eprint/56208

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