ArticleScientific reports2013
Tetraspanin-13 modulates voltage-gated CaV2.2 Ca2+ channels.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 16 citations in OpenAlex.
- Identification ofPathogens (Basel, Switzerland) · 2021Article
- Tetraspanins as Potential Modulators of Glutamatergic Synaptic Function.Frontiers in molecular neuroscience · 2021Review
- Lateral habenula dysfunctions in Tm4sf2Neurobiology of disease · 2021Article
- Modulation of voltage-gated CaChannels (Austin, Tex.) · 2020Review
- Tetraspanin-7 regulation of L-type voltage-dependent calcium channels controls pancreatic β-cell insulin secretion.The Journal of physiology · 2020Article
- Four novel interaction partners demonstrate diverse modulatory effects on voltage-gated CaPflugers Archiv : European journal of physiology · 2019Article
- Cloning and molecular characterization ofMolecular biology research communications · 2018Article
- Surfen is a broad-spectrum calcium channel inhibitor with analgesic properties in mouse models of acute and chronic inflammatory pain.Pflugers Archiv : European journal of physiology · 2017Article
- The two-pore channel TPC1 is required for efficient protein processing through early and recycling endosomes.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Integration of voltage-gated Ca(2+) channels in a network of protein-interactions is a crucial requirement for proper regulation of channel activity. In this study, we took advantage of the specific properties of the yeast split-ubiquitin system to search for and characterize so far unknown interaction partners of CaV2 Ca(2+) channels. We identified tetraspanin-13 (TSPAN-13) as an interaction partner of the α1 subunit of N-type CaV2.2, but not of P/Q-type CaV2.1 or L- and T-type Ca(2+) channels. Interaction could be located between domain IV of CaV2.2 and transmembrane segments S1 and S2 of TSPAN-13. Electrophysiological analysis revealed that TSPAN-13 specifically modulates the efficiency of coupling between voltage sensor activation and pore opening of the channel and accelerates the voltage-dependent activation and inactivation of the Ba(2+) current through CaV2.2. These data indicate that TSPAN-13 might regulate CaV2.2 Ca(2+) channel activity in defined synaptic membrane compartments and thereby influences transmitter release.
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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.