Evidence map›Paper›PMID 19596049›Full record

ArticleNeuroscience letters2009

The voltage-gated Na+ channel beta3 subunit does not mediate trans homophilic cell adhesion or associate with the cell adhesion molecule contactin.

Dyke P McEwen, Chunling Chen, Laurence S Meadows, Luis Lopez-Santiago, Lori L Isom

Open access · greenAbstract read
In one paragraph

Article in Neuroscience letters, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.2field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Voltage-Gated Na+ Channels: Not Just for Conduction.Cold Spring Harbor perspectives in biology · 2016
    Review
  11. Article
  12. Analgesic-antitumor peptide inhibits the migration and invasion of HepG2 cells by an upregulated VGSC β1 subunit.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  13. Dual roles of voltage-gated sodium channels in development and cancer.The International journal of developmental biology · 2015
    Review
  14. Review
  15. Review
  16. The immunoglobulin domain of the sodium channel β3 subunit contains a surface-localized disulfide bond that is required for homophilic binding.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  17. Article
  18. Article
  19. Voltage-gated Na+ channel β1B: a secreted cell adhesion molecule involved in human epilepsy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Dyke P McEwenDepartment of Pharmacology, University of Michigan, Ann Arbor, MI 48109-5632, USA.
Chunling Chen
Laurence S Meadows
Luis Lopez-Santiago
Lori L Isom
University of Michigan–Ann Arbor · US

Funding

INTERDEPARTMENTAL TRAINING IN PHARMACOLOGICAL SCIENCEST32GM007767 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ISOM, LORI L. · 1985 to 2019
$10.2M
Sodium Channel Beta Subunit Cell Adhesive InteractionsR01MH059980 · NIMH · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ISOM, LORI L. · 2000 to 2010
$2.7M
Contactin Interactions with Sodium Channel B1 SubunitsF31NS043067 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MCEWEN, DYKE P · 2002 to 2004
$73k
NIGMS NIH HHS GM07767NIGMS NIH HHS T32 GM007767NIMH NIH HHS R01 MH059980NIMH NIH HHS R01MH59980NINDS NIH HHS F31 NS043067NINDS NIH HHS NS43067
6 · The paper itself

Abstract

Voltage-gated Na(+) channel (VGSC) beta1 and beta2 subunits are multifunctional, serving as both channel modulators and cell adhesion molecules (CAMs). The purpose of this study was to determine whether VGSC beta3 subunits function as CAMs. The beta3 extracellular domain is highly homologous to beta1, suggesting that beta3 may also be a functional CAM. We investigated the trans homophilic cell adhesive properties of beta3, its association with the beta1-interacting CAM contactin, as well as its ability to interact with the cytoskeletal protein ankyrin. Our results demonstrate that, unlike beta1, beta3 does not participate in trans homophilic cell-cell adhesion or associate with contactin. Further, beta3 does not associate with ankyrin(G) in a heterologous system. Previous studies have shown that beta3 interacts with the CAM neurofascin-186 but not with VGSC beta1. Taken together, these findings suggest that, although beta1 and beta3 exhibit similar channel modulatory properties in heterologous systems, these subunits differ with regard to their homophilic and heterophilic CAM binding profiles.

Indexed as

AnimalsAnkyrinsCell AdhesionCell Adhesion MoleculesCell Adhesion Molecules, NeuronalCell LineContactinsCricetinaeCytoskeletal ProteinsDrosophilaFemalePatch-Clamp TechniquesProtein SubunitsRatsSodium ChannelsXenopus laevisAnkyrinsCell Adhesion MoleculesCell Adhesion Molecules, NeuronalContactinsCytoskeletal ProteinsProtein SubunitsSodium Channels

Identifiers

PMID19596049
PMCPMC2744945
OpenAlexW2043552203

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.