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

Membrane clustering and bungarotoxin binding by the nicotinic acetylcholine receptor: role of the ? subunit
Membrane clustering and bungarotoxin binding by the nicotinic acetylcholine receptor: role of the ? subunit
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 ? 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 ?1?1?? 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 ?1 subunit by the neuronal ?2 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 ?1?4?? 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 ?2. These results suggest that the ? subunit is an important determinant in receptor localisation and sensitivity to NBT.
? subunit, nicotinic, receptor clustering, xenopus oocytes, 43-kDa protein
0022-3042
1891-1899
Wheeler, Susan V.
ae7687e4-20ad-4d48-9263-390797c2b0e3
Jane, Steven D.
a4680c73-0947-4c61-8527-3345a09a849c
Cross, Kathryn M.L.
60843009-09b3-4a62-a180-4da0cee2272e
Chad, John E.
d220e55e-3c13-4d1d-ae9a-1cfae8ccfbe1
Foreman, Richard C.
5e7796fe-6411-4495-aa90-5f17d5d67ffa
Wheeler, Susan V.
ae7687e4-20ad-4d48-9263-390797c2b0e3
Jane, Steven D.
a4680c73-0947-4c61-8527-3345a09a849c
Cross, Kathryn M.L.
60843009-09b3-4a62-a180-4da0cee2272e
Chad, John E.
d220e55e-3c13-4d1d-ae9a-1cfae8ccfbe1
Foreman, Richard C.
5e7796fe-6411-4495-aa90-5f17d5d67ffa

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 ? subunit. Journal of Neurochemistry, 63 (5), 1891-1899. (doi:10.1046/j.1471-4159.1994.63051891.x).

Record type: Article

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 ? 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 ?1?1?? 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 ?1 subunit by the neuronal ?2 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 ?1?4?? 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 ?2. These results suggest that the ? subunit is an important determinant in receptor localisation and sensitivity to NBT.

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More information

Published date: 1 November 1994
Keywords: ? subunit, nicotinic, receptor clustering, xenopus oocytes, 43-kDa protein

Identifiers

Local EPrints ID: 56208
URI: http://eprints.soton.ac.uk/id/eprint/56208
ISSN: 0022-3042
PURE UUID: 4ceef32e-9a21-4ba3-b3d8-39dfc301deb4
ORCID for John E. Chad: ORCID iD orcid.org/0000-0001-6442-4281

Catalogue record

Date deposited: 22 Aug 2008
Last modified: 16 Mar 2024 02:35

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Contributors

Author: Susan V. Wheeler
Author: Steven D. Jane
Author: Kathryn M.L. Cross
Author: John E. Chad ORCID iD
Author: Richard C. Foreman

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