SCN- induces prestin contraction through reduced intermonomer angles and a modified transporter like movement of each monomer.

Prestin adopts increasingly contracted states in the presence of SCN-, driven by reduced intermonomer angles and cytoplasmic-half transmembrane contraction of each monomer.

• Why it matters: Voltage-linked electromotility depends on how prestin couples transporter-cycle conformations to membrane expansion and contraction, which remains unclear.
• What they did: Using ligand-dependent structural analysis, the study reports SCN-–specific conformational changes, including loss of the N-terminal intermonomer beta sheet and a hyperpolarizing shift in Vh with increased SCN- affinity.
• The result: SCN- binding at the internal site likely triggers these structural changes, which are reversed when SCN- is displaced by salicylate.

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