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Related Experiment Video

Updated: Jun 16, 2026

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels

Published on: July 4, 2016

Conformational state-dependent anion binding in prestin: evidence for allosteric modulation.

Lei Song¹, Joseph Santos-Sacchi

¹Department of Surgery (Otolaryngology), Yale University School of Medicine, New Haven, Connecticut, USA.

Biophysical Journal

|February 10, 2010

Summary

Anions allosterically regulate prestin, the motor protein in outer hair cells. Anion release during prestin expansion challenges existing models of auditory function.

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Area of Science:

Auditory Neuroscience
Molecular Biophysics
Cellular Electrophysiology

Background:

Outer hair cells (OHCs) are crucial for mammalian hearing, amplifying sound via somatic electromotility.
This electromotility is driven by prestin, an intramembranous molecular motor embedded in the OHC membrane.
Understanding prestin's function requires investigating the factors influencing its conformational changes and activity.

Purpose of the Study:

To investigate the role of anions in modulating prestin's activity and conformational states.
To determine how anion affinity changes with prestin's state under various biophysical conditions.
To challenge and refine existing models of prestin's voltage-sensing mechanism.

Main Methods:

Nonlinear capacitance measurements to assess prestin's electrical signature and electromotility.
Perturbation of membrane tension, temperature, and voltage to induce different prestin conformational states.
Analysis of anion binding affinity across these varied prestin states.

Main Results:

Anion affinity for prestin is state-dependent, varying with membrane tension, temperature, and voltage.
Prestin's expansion into its active state significantly reduces its affinity for anions.
Anions are released from prestin during expansion (hyperpolarization), contradicting the extrinsic voltage sensor model.

Conclusions:

Anions exert allosteric control over prestin function, binding and releasing in response to conformational changes.
The observed anion release mechanism during prestin expansion refutes the model of intracellular anions being propelled into the membrane.
Anion interactions likely contribute to prestin's susceptibility to biophysical forces and its piezoelectric properties.