A stepwise mechanism for acetylcholine receptor channel gating

Prasad Purohit, Ananya Mitra and Anthony Auerbach ()
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Prasad Purohit: State University of New York at Buffalo, Buffalo, New York 14214, USA
Ananya Mitra: State University of New York at Buffalo, Buffalo, New York 14214, USA
Anthony Auerbach: State University of New York at Buffalo, Buffalo, New York 14214, USA

Nature, 2007, vol. 446, issue 7138, 930-933

Abstract: Abstract Muscle contraction is triggered by the opening of acetylcholine receptors at the vertebrate nerve–muscle synapse1,2,3,4. The M2 helix of this allosteric membrane protein lines the channel, and contains a ‘gate’ that regulates the flow of ions through the pore. We used single-molecule kinetic analysis to probe the transition state of the gating conformational change and estimate the relative timing of M2 motions in the α-subunit of the murine acetylcholine receptor5. This analysis produces a ‘Φ-value’ for a given residue that reflects its open-like versus closed-like character at the transition state. Here we show that most of the residues throughout the length of M2 have a Φ-value of ∼0.64 but that some near the middle have lower Φ-values of 0.52 or 0.31, suggesting that αM2 moves in three discrete steps. The core of the channel serves both as a gate that regulates ion flow and as a hub that directs the propagation of the gating isomerization through the membrane domain of the acetylcholine receptor.

Date: 2007
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DOI: 10.1038/nature05721

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