ArticleThe Journal of biological chemistry2012
Calcium currents are enhanced by α2δ-1 lacking its membrane anchor.
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 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 39 citations in OpenAlex.
- Review
- Biochemistry and physiology of voltage-gated calcium channel trafficking: a target for gabapentinoid drugs.Open biology · 2025Review
- Rat Sympathetic Neuron Calcium Channels Are Insensitive to Gabapentin.Pharmaceuticals (Basel, Switzerland) · 2024Article
- The importance of cache domains in αChannels (Austin, Tex.) · 2023Article
- Depleted Calcium Stores and Increased Calcium Entry in Rod Photoreceptors of theInternational journal of molecular sciences · 2022Article
- ADAM17 Mediates Proteolytic Maturation of Voltage-Gated Calcium Channel Auxiliary αFunction (Oxford, England) · 2022Article
- More than a pore: How voltage-gated calcium channels act on different levels of neuronal communication regulation.Channels (Austin, Tex.) · 2021Review
- Rab11-dependent recycling of calcium channels is mediated by auxiliary subunit αScientific reports · 2021Article
- The life cycle of voltage-gated CaNeuronal signaling · 2021Review
- Direct, gabapentin-insensitive interaction of a soluble form of the calcium channel subunit αScientific reports · 2019Article
- The αCell reports · 2018Article
- Proteolytic maturation of αeLife · 2018Article
- The α2δ-1-NMDA Receptor Complex Is Critically Involved in Neuropathic Pain Development and Gabapentin Therapeutic Actions.Cell reports · 2018Article
- Voltage-gated calcium channel αF1000Research · 2018Review
- CaChannels (Austin, Tex.) · 2017Article
- Proteolytic cleavage of the hydrophobic domain in the CaThe Journal of biological chemistry · 2017Article
- LRP1 influences trafficking of N-type calcium channels via interaction with the auxiliary αScientific reports · 2017Article
- Proteolytic maturation of αeLife · 2016Article
- Voltage-gated calcium channels and their auxiliary subunits: physiology and pathophysiology and pharmacology.The Journal of physiology · 2016Review
- Dynamic association of calcium channel subunits at the cellular membrane.Neurophotonics · 2016Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The accessory α(2)δ subunits of voltage-gated calcium channels are membrane-anchored proteins, which are highly glycosylated, possess multiple disulfide bonds, and are post-translationally cleaved into α(2) and δ. All α(2)δ subunits have a C-terminal hydrophobic, potentially trans-membrane domain and were described as type I transmembrane proteins, but we found evidence that they can be glycosylphosphatidylinositol-anchored. To probe further the function of membrane anchoring in α(2)δ subunits, we have now examined the properties of α(2)δ-1 constructs truncated at their putative glycosylphosphatidylinositol anchor site, located before the C-terminal hydrophobic domain (α(2)δ-1ΔC-term). We find that the majority of α(2)δ-1ΔC-term is soluble and secreted into the medium, but unexpectedly, some of the protein remains associated with detergent-resistant membranes, also termed lipid rafts, and is extrinsically bound to the plasma membrane. Furthermore, heterologous co-expression of α(2)δ-1ΔC-term with Ca(V)2.1/β1b results in a substantial enhancement of the calcium channel currents, albeit less than that produced by wild-type α(2)δ-1. These results call into question the role of membrane anchoring of α(2)δ subunits for calcium current enhancement.
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Registered trials
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.