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Details on Person The membrane protein Slc26a5 (prestin) contracts in the plan...
| Class:Id | Summation:9667688 |
|---|---|
| _displayName | The membrane protein Slc26a5 (prestin) contracts in the plan... |
| _timestamp | 2020-07-12 11:05:48 |
| created | [InstanceEdit:9667732] May, Bruce, 2019-11-16 |
| modified | [InstanceEdit:9670755] May, Bruce, 2019-12-14 [InstanceEdit:9695276] May, Bruce, 2020-07-12 |
| text | 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. |
| (summation) | [BlackBoxEvent:9663359] Slc26a5 changes conformation in response to depolarization [Mus musculus] |
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