ArticleBiophysical journal2001
Molecular determinants of inactivation within the I-II linker of alpha1E (CaV2.3) calcium channels.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Calcium and arrhythmogenesis.Physiological reviews · 2007Pooled it
- Inactivation of CaV1 and CaV2 channels.The Journal of general physiology · 2025Review
- Molecular insights into the gating mechanisms of voltage-gated calcium channel CaNature communications · 2023Article
- Regulation of Presynaptic Calcium Channels.Advances in neurobiology · 2023Article
- Calcium Channel Splice Variants and Their Effects in Brain and Cardiovascular Function.Advances in experimental medicine and biology · 2021Article
- Role of a conserved glutamine in the function of voltage-gated CaThe Journal of biological chemistry · 2018Article
- Stapled Voltage-Gated Calcium Channel (CaACS chemical neuroscience · 2017Article
- Cooperative activation of the T-type CaV3.2 channel: interaction between Domains II and III.The Journal of biological chemistry · 2013Article
- How "Pharmacoresistant" is Cav2.3, the Major Component of Voltage-Gated R-type Ca2+ Channels?Pharmaceuticals (Basel, Switzerland) · 2013Article
- Double mutant cycle analysis identified a critical leucine residue in the IIS4S5 linker for the activation of the Ca(V)2.3 calcium channel.The Journal of biological chemistry · 2011Article
- Cysteines in the loop between IS5 and the pore helix of Ca(V)3.1 are essential for channel gating.Pflugers Archiv : European journal of physiology · 2010Article
- Disruption of the IS6-AID linker affects voltage-gated calcium channel inactivation and facilitation.The Journal of general physiology · 2009Article
- The guanylate kinase domain of the beta-subunit of voltage-gated calcium channels suffices to modulate gating.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Mutations of nonconserved residues within the calcium channel alpha1-interaction domain inhibit beta-subunit potentiation.The Journal of general physiology · 2008Article
- Alanine-scanning mutagenesis defines a conserved energetic hotspot in the CaValpha1 AID-CaVbeta interaction site that is critical for channel modulation.Structure (London, England : 1993) · 2008Article
- Vascular calcium channels and high blood pressure: pathophysiology and therapeutic implications.Vascular pharmacology · 2006Review
- Molecular regions underlying the activation of low- and high-voltage activating calcium channels.European biophysics journal : EBJ · 2005Article
- Negatively charged residues in the N-terminal of the AID helix confer slow voltage dependent inactivation gating to CaV1.2.Biophysical journal · 2004Article
- Structure of a complex between a voltage-gated calcium channel beta-subunit and an alpha-subunit domain.Nature · 2004Article
- Functional roles of cytoplasmic loops and pore lining transmembrane helices in the voltage-dependent inactivation of HVA calcium channels.The Journal of physiology · 2004Review
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Voltage-dependent inactivation of CaV2.3 channels was investigated using point mutations in the beta-subunit-binding site (AID) of the I-II linker. The quintuple mutant alpha1E N381K + R384L + A385D + D388T + K389Q (NRADK-KLDTQ) inactivated like the wild-type alpha1E. In contrast, mutations of alpha1E at position R378 (position 5 of AID) into negatively charged residues Glu (E) or Asp (D) significantly slowed inactivation kinetics and shifted the voltage dependence of inactivation to more positive voltages. When co-injected with beta3, R378E inactivated with tau(inact) = 538 +/- 54 ms (n = 14) as compared with 74 +/- 4 ms (n = 21) for alpha1E (p < 0.001) with a mid-potential of inactivation E(0.5) = -44 +/- 2 mV (n = 10) for R378E as compared with E(0.5) = -64 +/- 3 mV (n = 9) for alpha1E. A series of mutations at position R378 suggest that positively charged residues could promote voltage-dependent inactivation. R378K behaved like the wild-type alpha1E whereas R378Q displayed intermediate inactivation kinetics. The reverse mutation E462R in the L-type alpha1C (CaV1.2) produced channels with inactivation properties comparable to alpha1E R378E. Hence, position 5 of the AID motif in the I-II linker could play a significant role in the inactivation of Ca(V)1.2 and CaV2.3 channels.
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