ArticleBiophysical journal2011
Single-channel monitoring of reversible L-type Ca(2+) channel Ca(V)α(1)-Ca(V)β subunit interaction.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Inhibitory effects on L- and N-type calcium channels by a novel CaNaunyn-Schmiedeberg's archives of pharmacology · 2022Article
- Role of High Voltage-Gated CaCells · 2021Review
- Single-Channel Resolution of the Interaction between C-Terminal CaBiophysical journal · 2019Article
- Stapled Voltage-Gated Calcium Channel (CaACS chemical neuroscience · 2017Article
- The role of auxiliary subunits for the functional diversity of voltage-gated calcium channels.Journal of cellular physiology · 2015Review
- Structure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channels.Frontiers in physiology · 2014Review
- Stable incorporation versus dynamic exchange of β subunits in a native Ca2+ channel complex.Journal of cell science · 2013Article
- Equal sensitivity of Cav1.2 and Cav1.3 channels to the opposing modulations of PKA and PKG in mouse chromaffin cells.The Journal of physiology · 2012Article
- Membrane-localized β-subunits alter the PIP2 regulation of high-voltage activated Ca2+ channels.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-dependent Ca(2+) channels are heteromultimers of Ca(V)α(1) (pore), Ca(V)β- and Ca(V)α(2)δ-subunits. The stoichiometry of this complex, and whether it is dynamically regulated in intact cells, remains controversial. Fortunately, Ca(V)β-isoforms affect gating differentially, and we chose two extremes (Ca(V)β(1a) and Ca(V)β(2b)) regarding single-channel open probability to address this question. HEK293α(1C) cells expressing the Ca(V)1.2 subunit were transiently transfected with Ca(V)α(2)δ1 alone or with Ca(V)β(1a), Ca(V)β(2b), or (2:1 or 1:1 plasmid ratio) combinations. Both Ca(V)β-subunits increased whole-cell current and shifted the voltage dependence of activation and inactivation to hyperpolarization. Time-dependent inactivation was accelerated by Ca(V)β(1a)-subunits but not by Ca(V)β(2b)-subunits. Mixtures induced intermediate phenotypes. Single channels sometimes switched between periods of low and high open probability. To validate such slow gating behavior, data were segmented in clusters of statistically similar open probability. With Ca(V)β(1a)-subunits alone, channels mostly stayed in clusters (or regimes of alike clusters) of low open probability. Increasing Ca(V)β(2b)-subunits (co-)expressed (1:2, 1:1 ratio or alone) progressively enhanced the frequency and total duration of high open probability clusters and regimes. Our analysis was validated by the inactivation behavior of segmented ensemble averages. Hence, a phenotype consistent with mutually exclusive and dynamically competing binding of different Ca(V)β-subunits is demonstrated in intact cells.
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