Matches in SemOpenAlex for { <https://semopenalex.org/work/W4384560147> ?p ?o ?g. }
Showing items 1 to 63 of
63
with 100 items per page.
- W4384560147 abstract "Prestin responds to transmembrane voltage fluctuations by changing its cross-sectional area, a process underlying the electromotility of outer hair cells and cochlear amplification. Prestin belongs to the SLC26 family of anion transporters yet is the only member capable of displaying electromotility. Prestin’s voltage-dependent conformational changes are driven by the putative displacement of residue R399 and a set of sparse charged residues within the transmembrane domain, following the binding of a Cl- anion at a conserved binding site formed by amino termini of the TM3 and TM10 helices. However, a major conundrum arises as to how an anion that binds in proximity to a positive charge (R399), can promote the voltage sensitivity of prestin. Using hydrogen-deuterium exchange mass spectrometry, we find that prestin displays an unstable anion-binding site, where folding of the amino termini of TM3 and TM10 is coupled to Cl- binding. This event shortens the TM3-TM10 electrostatic gap, thereby connecting the two helices such that TM3-anion-TM10 is pushed upwards by forces from the electric field, resulting in reduced cross-sectional area. These folding events upon anion-binding are absent in SLC26A9, a non-electromotile transporter closely related to prestin. We also observe helix fraying at prestin’s anion-binding site but cooperative unfolding of multiple lipid-facing helices, features that may promote prestin’s fast electromechanical rearrangements. These results highlight a novel role of the folding equilibrium of the anion-binding site, and helps define prestin’s unique voltage-sensing mechanism and electromotility." @default.
- W4384560147 created "2023-07-18" @default.
- W4384560147 creator A5045259945 @default.
- W4384560147 date "2023-07-17" @default.
- W4384560147 modified "2023-10-16" @default.
- W4384560147 title "eLife assessment: Folding of Prestin’s Anion-Binding Site and the Mechanism of Outer Hair Cell Electromotility" @default.
- W4384560147 doi "https://doi.org/10.7554/elife.89635.1.sa0" @default.
- W4384560147 hasPublicationYear "2023" @default.
- W4384560147 type Work @default.
- W4384560147 citedByCount "0" @default.
- W4384560147 crossrefType "peer-review" @default.
- W4384560147 hasAuthorship W4384560147A5045259945 @default.
- W4384560147 hasBestOaLocation W43845601471 @default.
- W4384560147 hasConcept C107824862 @default.
- W4384560147 hasConcept C118892022 @default.
- W4384560147 hasConcept C119599485 @default.
- W4384560147 hasConcept C12554922 @default.
- W4384560147 hasConcept C127413603 @default.
- W4384560147 hasConcept C170493617 @default.
- W4384560147 hasConcept C185592680 @default.
- W4384560147 hasConcept C20418707 @default.
- W4384560147 hasConcept C24530287 @default.
- W4384560147 hasConcept C2776545253 @default.
- W4384560147 hasConcept C2780898785 @default.
- W4384560147 hasConcept C515207424 @default.
- W4384560147 hasConcept C55493867 @default.
- W4384560147 hasConcept C8010536 @default.
- W4384560147 hasConcept C86803240 @default.
- W4384560147 hasConcept C93126451 @default.
- W4384560147 hasConcept C95444343 @default.
- W4384560147 hasConceptScore W4384560147C107824862 @default.
- W4384560147 hasConceptScore W4384560147C118892022 @default.
- W4384560147 hasConceptScore W4384560147C119599485 @default.
- W4384560147 hasConceptScore W4384560147C12554922 @default.
- W4384560147 hasConceptScore W4384560147C127413603 @default.
- W4384560147 hasConceptScore W4384560147C170493617 @default.
- W4384560147 hasConceptScore W4384560147C185592680 @default.
- W4384560147 hasConceptScore W4384560147C20418707 @default.
- W4384560147 hasConceptScore W4384560147C24530287 @default.
- W4384560147 hasConceptScore W4384560147C2776545253 @default.
- W4384560147 hasConceptScore W4384560147C2780898785 @default.
- W4384560147 hasConceptScore W4384560147C515207424 @default.
- W4384560147 hasConceptScore W4384560147C55493867 @default.
- W4384560147 hasConceptScore W4384560147C8010536 @default.
- W4384560147 hasConceptScore W4384560147C86803240 @default.
- W4384560147 hasConceptScore W4384560147C93126451 @default.
- W4384560147 hasConceptScore W4384560147C95444343 @default.
- W4384560147 hasLocation W43845601471 @default.
- W4384560147 hasOpenAccess W4384560147 @default.
- W4384560147 hasPrimaryLocation W43845601471 @default.
- W4384560147 hasRelatedWork W1969099004 @default.
- W4384560147 hasRelatedWork W2035593786 @default.
- W4384560147 hasRelatedWork W2043759425 @default.
- W4384560147 hasRelatedWork W2224953524 @default.
- W4384560147 hasRelatedWork W2341989100 @default.
- W4384560147 hasRelatedWork W2914502418 @default.
- W4384560147 hasRelatedWork W3170520863 @default.
- W4384560147 hasRelatedWork W3191615877 @default.
- W4384560147 hasRelatedWork W4225566870 @default.
- W4384560147 hasRelatedWork W4235062674 @default.
- W4384560147 isParatext "false" @default.
- W4384560147 isRetracted "false" @default.
- W4384560147 workType "peer-review" @default.