ArticleThe Journal of general physiology2001
Altered state dependence of c-type inactivation in the long and short forms of human Kv1.5.
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 19 papers.
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Who cites it
19 citing papers in PubMed.
- Unmasking subtype-dependent susceptibility to C-type inactivation in mammalian Kv1 channels.Biophysical journal · 2024Article
- The N terminus and transmembrane segment S1 of Kv1.5 can coassemble with the rest of the channel independently of the S1-S2 linkage.The Journal of biological chemistry · 2018Article
- Inhibitory effects of cholinesterase inhibitor donepezil on the Kv1.5 potassium channel.Scientific reports · 2017Article
- Use-dependent activation of neuronal Kv1.2 channel complexes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
- The tetramerization domain potentiates Kv4 channel function by suppressing closed-state inactivation.Biophysical journal · 2014Article
- Role of outer-pore residue Y380 in U-type inactivation of KV2.1 channels.The Journal of membrane biology · 2013Article
- Voltage sensor inactivation in potassium channels.Frontiers in pharmacology · 2012Article
- Molecular determinants of U-type inactivation in Kv2.1 channels.Biophysical journal · 2011Article
- Mechanisms of closed-state inactivation in voltage-gated ion channels.The Journal of physiology · 2011Review
- Dependence of 6beta-acetoxy-7alpha-hydroxyroyleanone block of Kv1.2 channels on C-type inactivation.Cellular and molecular life sciences : CMLS · 2010Article
- Structural dynamics of an isolated voltage-sensor domain in a lipid bilayer.Structure (London, England : 1993) · 2008Article
- An activation gating switch in Kv1.2 is localized to a threonine residue in the S2-S3 linker.Biophysical journal · 2007Article
- An inactivation gate in the selectivity filter of KCNQ1 potassium channels.Biophysical journal · 2007Article
- Differential expression of potassium currents in Deiters cells of the guinea pig cochlea.Pflugers Archiv : European journal of physiology · 2006Article
- Short-term regulation of information processing at the corticoaccumbens synapse.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- Separation of P/C- and U-type inactivation pathways in Kv1.5 potassium channels.The Journal of physiology · 2005Article
- K+ currents activated by depolarization in cardiac fibroblasts.Biophysical journal · 2005Article
- NH2-terminal inactivation peptide binding to C-type-inactivated Kv channels.The Journal of general physiology · 2004Article
- Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition.The Journal of general physiology · 2003Article
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Evidence from both human and murine cardiomyocytes suggests that truncated isoforms of Kv1.5 can be expressed in vivo. Using whole-cell patch-clamp recordings, we have characterized the activation and inactivation properties of Kv1.5DeltaN209, a naturally occurring short form of human Kv1.5 that lacks roughly 75% of the T1 domain. When expressed in HEK 293 cells, this truncated channel exhibited a V(1/2) of -19.5 +/- 0.9 mV for activation and -35.7 +/- 0.7 mV for inactivation, compared with a V(1/2) of -11.2 +/- 0.3 mV for activation and -0.9 +/- 1.6 mV for inactivation in full-length Kv.15. Kv1.5DeltaN209 channels exhibited several features rarely observed in voltage-gated K(+) channels and absent in full-length Kv1.5, including a U-shaped voltage dependence of inactivation and "excessive cumulative inactivation," in which a train of repetitive depolarizations resulted in greater inactivation than a continuous pulse. Kv1.5DeltaN209 also exhibited a stronger voltage dependence to recovery from inactivation, with the time to half-recovery changing e-fold over 30 mV compared with 66 mV in full-length Kv1.5. During trains of human action potential voltage clamps, Kv1.5DeltaN209 showed 30-35% greater accumulated inactivation than full-length Kv1.5. These results can be explained with a model based on an allosteric model of inactivation in Kv2.1 (Klemic, K.G., C.-C. Shieh, G.E. Kirsch, and S.W. Jones. 1998. Biophys. J. 74:1779-1789) in which an absence of the NH(2) terminus results in accelerated inactivation from closed states relative to full-length Kv1.5. We suggest that differential expression of isoforms of Kv1.5 may contribute to K(+) current diversity in human heart and many other tissues.
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