Prestin is the motor protein of cochlear outer hair cells. Its unique capability to perform direct, rapid and reciprocal electromechanical conversion depends on membrane potential and interaction with intracellular anions. How prestin senses the voltage change and interacts with anions is still unknown. Our three-dimensional model of prestin, using molecular dynamics simulations, predicts that prestin contains eight transmembrane spanning segments, two helical re-entry loops and that tyrosyl residues are the structural specialization of the molecule for the unique function of prestin. Using site-directed mutagenesis and electrophysiological techniques, we confirmed that residues Y367, Y486, Y501 and Y508 contribute to anion binding, interacting with intracellular anions through novel anion-π interactions. Such weak interactions, sensitive to voltage and mechanical stimulation, confer prestin with a unique capability to perform electromechanical and mechanoelectric conversions with exquisite sensitivity. This novel mechanism is completely different from all known mechanisms seen in ion channels, transporters and motor proteins.
This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 12 January 2016.
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#22,760,732
of 25,377,790 outputs
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#82,451
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#238,048
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Outputs of similar age from Journal of Biological Chemistry
#388
of 457 outputs
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