期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 111, 期 13, 页码 4868-4873出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1322123111
关键词
asymmetry; allostery; Slo1 channels
资金
- National Institutes of Health Grant [GM-081748]
- National Research Service Award [GM103138]
Many K+ channels are oligomeric complexes with intrinsic 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. Here, through patch-clamp recordings of channel population ensembles and also single channels, we examine regulation of the Ca2+- and voltage-activated large conductance Ca2+-activated K+ (BK) channel by associated gamma 1-subunits. Through expression of differing ratios of gamma 1: alpha-subunits, the results reveal an all-or-none functional regulation of BK channels by gamma-subunits: channels either exhibit a full gating shift or no shift at all. Furthermore, the gamma 1-induced shift exhibits a state-dependent labile behavior that recapitulates the fully shifted or unshifted behavior. The gamma 1-induced shift contrasts markedly to the incremental shifts in BK gating produced by 1-4 beta-subunits and adds a new layer of complexity to the mechanisms by which BK channel functional diversity is generated.
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