Functional regulation of BK potassium channels by γ1 auxiliary subunits

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Abstract
Significance: K + channels are oligomeric complexes that typically exhibit structural symmetry arising from the homo-tetrameric core of their pore-forming subunits. Allosteric regulation of tetramerically symmetric proteins, whether by intrinsic sensing domains or associated auxiliary subunits, often mirrors the fourfold structural symmetry, as is the case for regulation of large conductance Ca 2+ -activated K + (BK) channels by auxiliary β-subunits. Here we describe an all-or-none regulation of BK channels by auxiliary γ-subunits that requires that a single γ1-subunit (or complex) is sufficient to produce the full regulatory effect. The contrast between incremental gating shifts produced by 1–4 β-subunits and the γ1-induced all-or-none shifts expands the range of mechanisms available to generate functional diversity in BK channels.

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