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- Title
LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium.
- Authors
Jiusheng Yan; Aldrich, Richard W.
- Abstract
Large-conductance, voltage- and calcium-activated potassium (BK, or KCa1.1) channels are ubiquitously expressed in electrically excitable and non-excitable cells, either as α-subunit (BKα) tetramers or together with tissue specific auxiliary β-subunits (β1–β4). Activation of BK channels typically requires coincident membrane depolarization and elevation in free cytosolic Ca2+ concentration ([Ca2+]i), which are not physiological conditions for most non-excitable cells. Here we present evidence that in non-excitable LNCaP prostate cancer cells, BK channels can be activated at negative voltages without rises in [Ca2+]i through their complex with an auxiliary protein, leucine-rich repeat (LRR)-containing protein 26 (LRRC26). LRRC26 modulates the gating of a BK channel by enhancing the allosteric coupling between voltage-sensor activation and the channel’s closed–open transition. This finding reveals a novel auxiliary protein of a voltage-gated ion channel that gives an unprecedentedly large negative shift (∼−140 mV) in voltage dependence and provides a molecular basis for activation of BK channels at physiological voltages and calcium levels in non-excitable cells.
- Publication
Nature, 2010, Vol 466, Issue 7305, p513
- ISSN
0028-0836
- Publication type
Academic Journal
- DOI
10.1038/nature09162