ArticleThe Journal of physiology2006
The importance of occupancy rather than affinity of CaV(beta) subunits for the calcium channel I-II linker in relation to calcium channel function.
Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Article
- Small-molecule CaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Translocatable voltage-gated CaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Stapled Voltage-Gated Calcium Channel (CaACS chemical neuroscience · 2017Article
- Molecular Basis of the Membrane Interaction of the β2e Subunit of Voltage-Gated Ca(2+) Channels.Biophysical journal · 2015Article
- Structure and function of the β subunit of voltage-gated Ca²⁺ channels.Biochimica et biophysica acta · 2013Review
- A quartet of leucine residues in the guanylate kinase domain of CaVβ determines the plasma membrane density of the CaV2.3 channel.The Journal of biological chemistry · 2012Article
- Mechanism of auxiliary β-subunit-mediated membrane targeting of L-type (Ca(V)1.2) channels.The Journal of physiology · 2011Article
- The ß subunit of voltage-gated Ca2+ channels.Physiological reviews · 2010Review
- Molecular determinants of the CaVbeta-induced plasma membrane targeting of the CaV1.2 channel.The Journal of biological chemistry · 2010Article
- Reciprocal interactions regulate targeting of calcium channel beta subunits and membrane expression of alpha1 subunits in cultured hippocampal neurons.The Journal of biological chemistry · 2010Article
- CaMKII associates with CaV1.2 L-type calcium channels via selected beta subunits to enhance regulatory phosphorylation.Journal of neurochemistry · 2010Article
- Functional dissection of the intramolecular Src homology 3-guanylate kinase domain coupling in voltage-gated Ca2+ channel beta-subunits.FEBS letters · 2009Article
- Determinants of the voltage dependence of G protein modulation within calcium channel beta subunits.Pflugers Archiv : European journal of physiology · 2009Article
- Differential regulated interactions of calcium/calmodulin-dependent protein kinase II with isoforms of voltage-gated calcium channel beta subunits.Biochemistry · 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
- Functional modularity of the beta-subunit of voltage-gated Ca2+ channels.Biophysical journal · 2007Article
- Disrupting calcium channel expression to lower blood pressure: new targeting of a well-known channel.Molecular interventions · 2006Article
- The structural biology of voltage-gated calcium channel function and regulation.Biochemical Society transactions · 2006Article
- Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.Channels (Austin, Tex.)Review
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5 authors.
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Abstract
The Ca(V)beta subunits of voltage-gated calcium channels regulate the trafficking and biophysical properties of these channels. We have taken advantage of mutations in the tyrosine residue within the alpha interaction domain (AID) in the I-II linker of Ca(V)2.2 which reduce, but do not abolish, the binding of beta1b to the AID of Ca(V)2.2. We have found that the mutation Y388S decreased the affinity of Ca(V)beta1b binding to the Ca(V)2.2 I-II linker from 14 to 329 nm. However, the Y388S mutation had no effect on current density and cell surface expression of Ca(V)2.2/alpha2delta-2/beta1b channels expressed in human embryonic kidney tsA-201 cells, when equivalent proportions of cDNA were used. Furthermore, despite the 24-fold reduced affinity of Ca(V)beta1b for the Y388S I-II linker of Ca(V)2.2, all the key features of modulation as well as trafficking by Ca(V)beta subunits remained intact. This is in contrast to the much more marked effect of the W391A mutation, which abolished interaction with the Ca(V)2.2 I-II linker, and very markedly affected the trafficking of the channels. However, using the Xenopus oocyte expression system, where expression levels can be accurately titrated, when Ca(V)beta1b cDNA was diluted 50-fold, all evidence of interaction with Ca(V)2.2 Y388S was lost, although wild-type Ca(V)2.2 was still normally modulated by the reduced concentration of beta1b. These results indicate that high affinity interaction with the alpha1 subunit is not necessary for any of the modulatory effects of Ca(V)beta subunits, but occupancy of the interaction site is important, and this will occur, despite the reduced affinity, if the Ca(V)beta subunit is present in sufficient excess.
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