ArticleScientific reports2013
Interaction between the transcriptional corepressor Sin3B and voltage-gated sodium channels modulates functional channel expression.
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 7 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Experimental and computational evidence that Calpain-10 binds to the carboxy terminus of NaScientific reports · 2024Article
- Direct fluorescent labeling of NF186 and NaV1.6 in living primary neurons using bioorthogonal click chemistry.Journal of cell science · 2023Article
- Contributions of NaScientific reports · 2021Article
- Same agent, different messages: insight into transcriptional regulation by SIN3 isoforms.Epigenetics & chromatin · 2018Review
- Zebrafish sin3b mutants are viable but have size, skeletal, and locomotor defects.Developmental dynamics : an official publication of the American Association of Anatomists · 2017Article
- Transmembrane voltage potential of somatic cells controls oncogene-mediated tumorigenesis at long-range.Oncotarget · 2014Article
- Long-range gap junctional signaling controls oncogene-mediated tumorigenesis in Xenopus laevis embryos.Frontiers in physiology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Proteins that interact with voltage-gated sodium (Na(v)) channels are important in channel sorting and modulation. In this study, we identified the transcriptional regulator, Sin3B, as a novel binding partner of Na(v) channels in a yeast two-hybrid screen and confirmed the interaction using pull-down assays, co-immunoprecipitation, and immunofluorescence-colocalization. Because both long (~1100-residue) and short (N-terminal 293 residues) Sin3B variants interacted with Na(v) channels, binding occurred within the N-terminal region containing two paired-amphipathic helix domains. In Na(v) channels, Sin3B bound to a 132-residue portion of the cytoplasmic C-terminus. Expression of the short Sin3B variant strongly reduced native sodium current and Na(v)-channel gating charge in the neuronal cell line N1E-115, without affecting the voltage-dependence of activation. Because the total amount of channel protein was unchanged by Sin3B, binding of Sin3B likely decreases the number of channels in the plasma membrane, suggesting that interaction with Sin3B influences Na(v)-channel trafficking or stability in the membrane.
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Registered trials
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