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MacKenzie Thompson

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Articles

Asynchronous subunit transitions prime acetylcholine receptor activation

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By MacKenzie Thompson, Mackenzie Thompson, Anna Ananchenko, Camille Hénault, Johnathon R. Emlaw, Hugues Nury, John E Baenziger
| Science Magazine Verified
Abstract Communication at synapses is facilitated by postsynaptic receptors, which convert a chemical signal into an electrical response. For ligand-gated ion channels, agonist binding triggers rapid transitions through intermediate states leading to a transient open-pore conformation, with these transitions shaping the post-synaptic response. Here, we determine structures of the muscle-type nicotinic acetylcholine receptor in unliganded, mono-liganded, and di-liganded states.
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Asynchronous subunit transitions precede acetylcholine receptor activation

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By MacKenzie Thompson, Mackenzie Thompson, Johnathon R. Emlaw, Christian J.G. Tessier, Anna Ananchenko
| BioRxiv
Abstract Rapid communication at synapses is facilitated by postsynaptic receptors, which convert a chemical signal into an electrical response. In the case of ligand-gated ion channels, agonist binding triggers rapid transition through a series of intermediate states leading to a transient open-pore conformation. These transitions are usually framed in terms of a mechanism where agonist binding and channel activation are separate events.
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A release of local subunit conformational heterogeneity underlies gating in a muscle nicotinic acetylcholine receptor - Nature Communications

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By MacKenzie Thompson, Mackenzie Thompson, Farid Mansoub Bekarkhanechi
| Nature Verified
Abstract Synaptic receptors respond to neurotransmitters by opening an ion channel across the post-synaptic membrane to elicit a cellular response. Here we use recent Torpedo acetylcholine receptor structures and functional measurements to delineate a key feature underlying allosteric communication between the agonist-binding extracellular and channel-gating transmembrane domains.
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