Slc26a5 changes conformation in response to depolarization

Stable Identifier
Reaction [omitted]
Mus musculus
SVG |   | PPTX  | SBGN
Slc26a5 changes conformation in response to depolarization

The membrane protein Slc26a5 (prestin) contracts in the plane of the membrane in response to depolarization of the cell caused by opening of the mechanoelectric transduction (MET) channel (inferred from rat homologs). A current model for the reaction posits that association of anions (chloride or bicarbonate) with a binding pocket midway along the permeation pathway within Slc26a5 causes a change in the area occupied by Slc26a5 in the membrane. An influx of cations through the MET channel causes dissociation of anions from Slc26a5, reversing the conformational change. The contraction-elongation cycle of OHCs, due to conformational changes of Slc26a5, provides feedback-amplification of the motions (principally the reticular lamina) of the organ of Corti. At low sound levels the amplification is about a 1000-fold, decreasing nonlinearly as sound level increases. In the absence of either OHCs (Ryan and Dallos 1975) or functional Slc26a5 (Liberman et al. 2002, Cheatham et al. 2004, Dallos et al. 2008) the amplification disappears.

Literature References
PubMed ID Title Journal Year
18466744 Prestin-based outer hair cell motility is necessary for mammalian cochlear amplification

Dallos, P, Wu, X, Cheatham, MA, Gao, J, Zheng, J, Anderson, CT, Jia, S, Wang, X, Cheng, WH, Sengupta, S, He, DZ, Zuo, J

Neuron 2008
15319415 Cochlear function in Prestin knockout mice

Cheatham, MA, Huynh, KH, Gao, J, Zuo, J, Dallos, P

J. Physiol. (Lond.) 2004
12239568 Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier

Liberman, MC, Gao, J, He, DZ, Wu, X, Jia, S, Zuo, J

Nature 2002
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