Slc26a5 changes conformation in response to depolarization

Stable Identifier
R-RNO-9667710
Type
Reaction [omitted]
Species
Rattus norvegicus
Compartment
General
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 mechanoelectrical transduction (MET) channel (Oliver et al. 2001, Gorbunov et al. 2014). Likewise, Slc26a5 expands in the plane of the membrane in response to hyperpolarization caused by MET channel closing. 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 (Oliver et al. 2001, Gorbunov et al. 2014). An influx of cations through the MET channel causes dissociation of anions from Slc26a5, reversing the conformational change (Oliver et al. 2001, Gorbunov et al. 2014). The contraction-elongation cycle of OHCs, due to conformational changes of prestin, provides feedback-amplification of the motions (principally the reticular lamina) of the organ of Corti.

Literature References
PubMed ID Title Journal Year
24710176 Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters

Gorbunov, D, Sturlese, M, Nies, F, Kluge, M, Bellanda, M, Battistutta, R, Oliver, D

Nat Commun 2014
11423665 Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein

Oliver, D, He, DZ, Klöcker, N, Ludwig, J, Schulte, U, Waldegger, S, Ruppersberg, JP, Dallos, P, Fakler, B

Science 2001
Participants
Orthologous Events
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