ArticleThe Journal of general physiology1997
Role of the S3-S4 linker in Shaker potassium channel activation.
Article in The Journal of general physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 59 citations in OpenAlex.
- NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles.Biophysical journal · 2019Article
- Electrostatic Tuning of a Potassium Channel in Electric Fish.Current biology : CB · 2018Article
- Nonsensing residues in S3-S4 linker's C terminus affect the voltage sensor set point in KThe Journal of general physiology · 2018Article
- Linker flexibility of IVS3-S4 loops modulates voltage-dependent activation of L-type CaChannels (Austin, Tex.) · 2017Article
- Extracellular Linkers Completely Transplant the Voltage Dependence from Kv1.2 Ion Channels to Kv2.1.Biophysical journal · 2016Article
- The Molecular Basis of Polyunsaturated Fatty Acid Interactions with the Shaker Voltage-Gated Potassium Channel.PLoS computational biology · 2016Article
- S3-S4 linker length modulates the relaxed state of a voltage-gated potassium channel.Biophysical journal · 2013Article
- β4-subunit increases Slo responsiveness to physiological Ca2+ concentrations and together with β1 reduces surface expression of Slo in hair cells.American journal of physiology. Cell physiology · 2011Article
- Transfer of rolf S3-S4 linker to HERG eliminates activation gating but spares inactivation.Biophysical journal · 2009Article
- Developmental control of CaV1.2 L-type calcium channel splicing by Fox proteins.Molecular and cellular biology · 2009Article
- Potassium channel opening: a subtle two-step.The Journal of physiology · 2009Article
- Fluorescence detection of the movement of single KcsA subunits reveals cooperativity.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Structural basis for ether-a-go-go-related gene K+ channel subtype-dependent activation by niflumic acid.Molecular pharmacology · 2008Article
- A hydrophobic element secures S4 voltage sensor in position in resting Shaker K+ channels.The Journal of physiology · 2007Article
- Constraints on voltage sensor movement in the shaker K+ channel.The Journal of general physiology · 2006Article
- Molecular diversity and regulation of renal potassium channels.Physiological reviews · 2005Review
- Effects of Kv1.2 intracellular regions on activation of Kv2.1 channels.Biophysical journal · 2004Article
- Detecting rearrangements of shaker and NaChBac in real-time with fluorescence spectroscopy in patch-clamped mammalian cells.Biophysical journal · 2004Article
- Functional diversity in neuronal voltage-gated calcium channels by alternative splicing of Ca(v)alpha1.Molecular neurobiology · 2002Review
- Determinants of activation kinetics in mammalian hyperpolarization-activated cation channels.The Journal of physiology · 2001Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Structural models of voltage-gated channels suggest that flexibility of the S3-S4 linker region may be important in allowing the S4 region to undergo large conformational changes in its putative voltage-sensing function. We report here the initial characterization of 18 mutations in the S3-S4 linker of the Shaker channel, including deletions, insertions, charge change, substitution of prolines, and chimeras replacing the 25-residue Shaker linker with 7- or 9-residue sequences from Shab, Shaw, or Shal. As measured in Xenopus oocytes with a two-microelectrode voltage clamp, each mutant construct yielded robust currents. Changes in the voltage dependence of activation were small, with activation voltage shifts of 13 mV or less. Substitution of linkers from the slowly activating Shab and Shaw channels resulted in a three-to fourfold slowing of activation and deactivation. It is concluded that the S3-S4 linker is unlikely to participate in a large conformational change during channel activation. The linker, which in some channel subfamilies has highly conserved sequences, may however be a determinant of activation kinetics in potassium channels, as previously has been suggested in the case of calcium channels.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.