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Significance BEST1 is a Ca2+ -activated chloride channel found in a variety of cell types that allows chloride to traverse the plasma membrane. Mutations in BEST1 can cause macular degeneration. The mechanisms for anion selectivity and Ca2+ -dependent activation of BEST1 are unknown. Here, we show that a hydrophobic “neck” region of the channel’s pore does not play a major role in ion selectivity but acts as an effective gate, responding to Ca2+ binding at a cytosolic sensor. Mutation of a cytosolic “aperture” dramatically affects relative permeabilities among anions. These insights help rationalize how disease-causing mutations in BEST1 affect channel behavior and contribute to a broader understanding of ion channel gating and selectivity mechanisms.

Distinct regions that control ion selectivity and calcium-dependent activation in the bestrophin ion channel