ArticleThe Journal of general physiology2001
Gating properties conferred on BK channels by the beta3b auxiliary subunit in the absence of its NH(2)- and COOH termini.
Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- An extracellular scaffolding complex confers unusual rectification upon an ionotropic acetylcholine receptor inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- A voltage-dependent KThe Journal of cell biology · 2017Article
- Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- Inter-α/β subunits coupling mediating pre-inactivation and augmented activation of BKCa(β2).Scientific reports · 2013Article
- The BK channel: a vital link between cellular calcium and electrical signaling.Protein & cell · 2012Review
- Modulation of BK channel voltage gating by different auxiliary β subunits.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Barium ions selectively activate BK channels via the Ca2+-bowl site.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Contribution of BK channels to action potential repolarisation at minimal cytosolic Ca2+ concentration in chromaffin cells.Pflugers Archiv : European journal of physiology · 2011Article
- Species-specific Differences among KCNMB3 BK beta3 auxiliary subunits: some beta3 N-terminal variants may be primate-specific subunits.The Journal of general physiology · 2008Article
- Lysine-rich extracellular rings formed by hbeta2 subunits confer the outward rectification of BK channels.PloS one · 2008Article
- Slo3 K+ channels: voltage and pH dependence of macroscopic currents.The Journal of general physiology · 2006Article
- Defining the BK channel domains required for beta1-subunit modulation.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Structural determinants for functional coupling between the beta and alpha subunits in the Ca2+-activated K+ (BK) channel.The Journal of general physiology · 2006Article
- Differential effects of beta 1 and beta 2 subunits on BK channel activity.The Journal of general physiology · 2005Article
- The BKCa channel's Ca2+-binding sites, multiple sites, multiple ions.The Journal of general physiology · 2005Review
- Divalent cation sensitivity of BK channel activation supports the existence of three distinct binding sites.The Journal of general physiology · 2005Article
- Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues.The Journal of general physiology · 2003Article
- Gating mechanism of BK (Slo1) channels: so near, yet so far.The Journal of general physiology · 2003Review
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4 authors.
Funding
Abstract
Both beta1 and beta2 auxiliary subunits of the BK-type K(+) channel family profoundly regulate the apparent Ca(2)+ sensitivity of BK-type Ca(2)+-activated K(+) channels. Each produces a pronounced leftward shift in the voltage of half-activation (V(0.5)) at a given Ca(2)+ concentration, particularly at Ca(2)+ above 1 microM. In contrast, the rapidly inactivating beta3b auxiliary produces a leftward shift in activation at Ca(2)+ below 1 microM. In the companion work (Lingle, C.J., X.-H. Zeng, J.-P. Ding, and X.-M. Xia. 2001. J. Gen. Physiol. 117:583-605, this issue), we have shown that some of the apparent beta3b-mediated shift in activation at low Ca(2)+ arises from rapid unblocking of inactivated channels, unlike the actions of the beta1 and beta2 subunits. Here, we compare effects of the beta3b subunit that arise from inactivation, per se, versus those that may arise from other functional effects of the subunit. In particular, we examine gating properties of the beta3b subunit and compare it to beta3b constructs lacking either the NH(2)- or COOH terminus or both. The results demonstrate that, although the NH(2) terminus appears to be the primary determinant of the beta3b-mediated shift in V(0.5) at low Ca(2)+, removal of the NH(2) terminus reveals two other interesting aspects of the action of the beta3b subunit. First, the conductance-voltage curves for activation of channels containing the beta3b subunit are best described by a double Boltzmann shape, which is proposed to arise from two independent voltage-dependent activation steps. Second, the presence of the beta3b subunit results in channels that exhibit an anomalous instantaneous outward current rectification that is correlated with a voltage dependence in the time-averaged single-channel current. The two effects appear to be unrelated, but indicative of the variety of ways that interactions between beta and alpha subunits can affect BK channel function. The COOH terminus of the beta3b subunit produces no discernible functional effects.
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