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Significance Voltage-sensing phosphatase (VSP) dephosphorylates phosphoinositides in a voltage-dependent manner. The molecular mechanisms by which the voltage-sensor domain of VSP activates the catalytic activity of the cytoplasmic region still remain unknown. Using a method of incorporation of a fluorescent unnatural amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), in the catalytic region, we revealed that some loops in the catalytic region move on membrane depolarization and that the catalytic region is located beneath the plasma membrane irrespective of the membrane potential. Furthermore, fluorescence change of Anap in the C2 domain showed multiple voltage-dependent activated states and protein conformation, which is sensitive to substrate availability in the active center. These findings provide novel insights into the mechanisms of voltage-dependent catalytic activity of VSP.

Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid