NDLI: β1 subunits facilitate gating of BK channels by acting through the $Ca^{2+},$ but not the $Mg^{2+},$ activating mechanisms

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β1 subunits facilitate gating of BK channels by acting through the $Ca^{2+},$ but not the $Mg^{2+},$ activating mechanisms

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β1 subunits facilitate gating of BK channels by acting through the $Ca^{2+},$ but not the $Mg^{2+},$ activating mechanisms

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Qian, Xiang Magleby, Karl L.
Description	Author Affiliation: Qian X ( Department of Physiology and Biophysics, University of Miami School of Medicine, 1600 Northwest 10th Avenue, Miami, FL 33136, USA.);
Abstract	The beta1 subunit of BK (large conductance Ca2+ and voltage-activated K+) channels is essential for many key physiological processes, such as controlling the contraction of smooth muscle and the tuning of hair cells in the cochlea. Although it is known that the beta1 subunit greatly increases the open probability of BK channels, little is known about its mechanism of action. We now explore this mechanism by using channels in which the Ca2+- and Mg2+-dependent activating mechanisms have been disrupted by mutating three sites to remove the Ca2+ and Mg2+ sensitivity. We find that the presence of the beta1 subunit partially restores Ca2+ sensitivity to the triply mutated channels, but not the Mg2+ sensitivity. We also find that the beta1 subunit has no effect on the Mg2+ sensitivity of WT BK channels, in contrast to its pronounced effect of increasing the apparent Ca2+ sensitivity. These observations suggest that the beta1 subunit increases open probability by working through the Ca2+-dependent, rather than Mg2+-dependent, activating mechanisms, and that the action of the beta1 subunit is not directly on the Ca2+ binding sites, but on the allosteric machinery coupling the sites to the gate. The differential effects of the beta1 subunit on the Ca2+ and Mg2+ activation of the channel suggest that these processes act separately. Finally, we show that Mgi2+ inhibits, rather than activates, BK channels in the presence of the beta1 subunit for intermediate levels of Cai2+. This Mg2+ inhibition in the presence of the beta1 subunit provides an additional regulatory mechanism of BK channel activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Metabolism Magnesium Potassium Channels, Calcium-Activated Chemistry Animals Binding Sites Genetics Pharmacology In Vitro Techniques Ion Channel Gating Kinetics Large-Conductance Calcium-Activated Potassium Channels Mice Mutagenesis, Site-Directed Oocytes Drug Effects Protein Subunits Recombinant Proteins Xenopus Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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