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- W2912797267 abstract "Molecular identification of ion channels that mediate sensory transduction has been a major focus in the field of sensory biology for many years, yet, the proteins that form sensory transduction channels required for hearing and balance have not been definitively identified. TMC1 and TMC2 have been proposed as possible pore-forming subunits, but the pore region itself has not been identified. We generated 17 unique cysteine substitutions in TMC1 and packaged the mutant sequences into AAV2/1 vectors. The vectors were injected into the inner ears of P1 mice that lacked expression of endogenous Tmc1 and Tmc2. Injected ears were dissected at P7 and the organ of Corti was cultured for an additional 8 to 10 days. We used rapid hair bundle deflections and the whole-cell, tight-seal technique to record sensory transduction currents from 566 inner hair cells. We applied four different cysteine modification reagents methanethiosulfonate (MTS) to native mouse sensory hair cells. We identified thirteen TMC1 residues that altered the biophysical properties of hair cell mechanosensory transduction. Five residues were rapidly modified by MTS reagents to confer changes in whole-cell current amplitudes. Three sites examined in detail, caused changes in single-channel current amplitudes. Eleven sites altered calcium selectivity and cysteine substitution at one site blocked current almost entirely. The data support a revised TMC1 topology with ten transmembrane domains and identify four TMC1 transmembrane domains that line the permeation pathway of mechanosensory transduction channels in mammalian auditory and vestibular hair cells. We conclude TMC1 is a major pore-forming subunit of the hair cell sensory transduction channel." @default.
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- W2912797267 date "2019-02-01" @default.
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- W2912797267 title "Cysteine Substitution Reveals the Pore-Forming Region of TMC1 in Hair Cell Sensory Transduction Channels" @default.
- W2912797267 doi "https://doi.org/10.1016/j.bpj.2018.11.2486" @default.
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