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Published on: July 1, 2021
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Progress in understanding the structural mechanism underlying prestin's electromotile activity.
Dominik Lenz1, Dominik Oliver2
1Institute for Physiology and Pathophysiology, Philipps University Marburg, Deutschhausstr. 2, Marburg 35037, Germany.
Hearing Research
|January 6, 2022
Summary
Prestin, the motor protein driving outer hair cell (OHC) electromotility, undergoes voltage-dependent conformational changes. Recent cryo-EM structures reveal prestin
Area of Science:
- Molecular Biophysics
- Structural Biology
- Cellular Physiology
Background:
- Prestin (SLC26A5) is the key molecular actuator responsible for outer hair cell (OHC) electromotility (eM).
- Electromotility is driven by an area motor mechanism where prestin molecules change membrane area in response to voltage.
- Understanding prestin's structural dynamics has been limited by a lack of high-resolution structural data.
Purpose of the Study:
- To review recent cryo-electron microscopy (cryo-EM) structures of prestin and other SLC26 transporters.
- To discuss insights into the molecular mechanism underlying prestin's function and electromotility.
- To explore how structural rearrangements in prestin may contribute to membrane deformation and eM.
Main Methods:
- Analysis of high-resolution cryo-EM structures of prestin and related SLC26 transporters.
- Comparison of prestin structures in different conformational states, bound to various anions.
- Review of biophysical data and theoretical models of OHC electromotility.
Main Results:
- SLC26 transporters, including prestin, form dimers with a 7+7 transmembrane domain inverted repeat (7TMIR) architecture.
- Distinct prestin conformations were observed, differing in the area occupied by the transmembrane domain (TMD) and its lipid environment.
- These conformational changes, involving core and scaffold domains, impact membrane area and may underlie electromotility.
Conclusions:
- Recent structural data provide a reliable picture of prestin's molecular architecture and conformational landscape.
- Prestin's voltage-driven conformational rearrangements, affecting membrane area and lipid interactions, are likely key to electromotility.
- Further functional studies are needed to confirm the direct link between these structural dynamics and piezoelectric activity.
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