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JGP study shows that hydrophobic residues in the S1 transmembrane domain modulate the voltage-sensor movements and enzymatic activity of voltage-sensing phosphatase.


Rayaprolu et al. investigated how hydrophobic residues impact the function of the voltage-sensing phosphatase. They mutated different positions in the S1 helix of the voltage-sensing domain and found more energy was needed for enzyme activation while less was needed to move the sensor.

In a screen of 10,000 compounds, Ronnelid and Elinder found that carboxyl-group–containing compounds are potent activators of voltage-gated potassium channels. They suggest that lipophilic and charged compounds electrostatically activate the channel by binding close to the channel’s voltage sensor.

Niclosamide, a proposed TMEM16A inhibitor for asthma and COPD, unexpectedly enhances TMEM16A activity, raising caution for its clinical use. Discovering its binding site on TMEM16A aids in developing targeted modulators for various diseases.

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