ArticleThe Journal of biological chemistry2012
A quartet of leucine residues in the guanylate kinase domain of CaVβ determines the plasma membrane density of the CaV2.3 channel.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Epilepsy-linked kinase CDKL5 phosphorylates voltage-gated calcium channel Cav2.3, altering inactivation kinetics and neuronal excitability.Nature communications · 2023Article
- Sympathetic Stimulation Upregulates the CaCells · 2022Article
- A three-way inter-molecular network accounts for the CaThe Journal of biological chemistry · 2018Article
- Negatively charged residues in the first extracellular loop of the L-type CaThe Journal of biological chemistry · 2017Article
- Proteolytic cleavage of the hydrophobic domain in the CaThe Journal of biological chemistry · 2017Article
- Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry.Journal of visualized experiments : JoVE · 2016Article
- Identification of Glycosylation Sites Essential for Surface Expression of the CaVα2δ1 Subunit and Modulation of the Cardiac CaV1.2 Channel Activity.The Journal of biological chemistry · 2016Article
- Review: CaThe open neurology journal · 2016Article
- Functional characterization of CaVα2δ mutations associated with sudden cardiac death.The Journal of biological chemistry · 2015Article
- 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
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Ca(V)β subunits are formed by a Src homology 3 domain and a guanylate kinase-like (GK) domain connected through a variable HOOK domain. Complete deletion of the Src homology 3 domain (75 residues) as well as deletion of the HOOK domain (47 residues) did not alter plasma membrane density of Ca(V)2.3 nor its typical activation gating. In contrast, six-residue deletions in the GK domain disrupted cell surface trafficking and functional expression of Ca(V)2.3. Mutations of residues known to carry nanomolar affinity binding in the GK domain of Ca(V)β (P175A, P179A, M195A, M196A, K198A, S295A, R302G, R307A, E339G, N340G, and A345G) did not significantly alter cell surface targeting or gating modulation of Ca(V)2.3. Nonetheless, mutations of a quartet of leucine residues (either single or multiple mutants) in the α3, α6, β10, and α9 regions of the GK domain were found to significantly impair cell surface density of Ca(V)2.3 channels. Furthermore, the normalized protein density of Ca(V)2.3 was nearly abolished with the quadruple Ca(V)β3 Leu mutant L200G/L303G/L337G/L342G. Altogether, our observations suggest that the four leucine residues in Ca(V)β3 form a hydrophobic pocket surrounding key residues in the α-interacting domain of Ca(V)2.3. This interaction appears to play an essential role in conferring Ca(V)β-induced modulation of the protein density of Ca(V)α1 subunits in Ca(V)2 channels.
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