Evidence map›Paper›PMID 24273166›Full record

ArticleThe Journal of biological chemistry2014

Latrophilins function as heterophilic cell-adhesion molecules by binding to teneurins: regulation by alternative splicing.

Antony A Boucard, Stephan Maxeiner, Thomas C Südhof

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

133 citing papers in PubMed, 193 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  8. EndothelialThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2026
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Complex G-protein signaling of the adhesion GPCR, ADGRA3.The Journal of biological chemistry · 2025
    Article
  18. Article
  19. Article
  20. Article

73 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Antony A BoucardFrom the Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Palo Alto, California 94305.
Stephan Maxeiner
Thomas C Südhof
Stanford University · US

Funding

FUNCTION OF NEUREXINSR37MH052804 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI SUDHOF, THOMAS C. · 2000 to 2019
$9.3M
Large-Scale Molecular Interrogation of Synaptic TransmissionR01NS077906 · NINDS · STANFORD UNIVERSITY · PI CHEN, LU, MALENKA, ROBERT C · 2011 to 2014
$2.5M
NIMH NIH HHS R37 MH052804NINDS NIH HHS R01 NS077906
6 · The paper itself

Abstract

Latrophilin-1, -2, and -3 are adhesion-type G protein-coupled receptors that are auxiliary α-latrotoxin receptors, suggesting that they may have a synaptic function. Using pulldowns, we here identify teneurins, type II transmembrane proteins that are also candidate synaptic cell-adhesion molecules, as interactors for the lectin-like domain of latrophilins. We show that teneurin binds to latrophilins with nanomolar affinity and that this binding mediates cell adhesion, consistent with a role of teneurin binding to latrophilins in trans-synaptic interactions. All latrophilins are subject to alternative splicing at an N-terminal site; in latrophilin-1, this alternative splicing modulates teneurin binding but has no effect on binding of latrophilin-1 to another ligand, FLRT3. Addition to cultured neurons of soluble teneurin-binding fragments of latrophilin-1 decreased synapse density, suggesting that latrophilin binding to teneurin may directly or indirectly influence synapse formation and/or maintenance. These observations are potentially intriguing in view of the proposed role for Drosophila teneurins in determining synapse specificity. However, teneurins in Drosophila were suggested to act as homophilic cell-adhesion molecules, whereas our findings suggest a heterophilic interaction mechanism. Thus, we tested whether mammalian teneurins also are homophilic cell-adhesion molecules, in addition to binding to latrophilins as heterophilic cell-adhesion molecules. Strikingly, we find that although teneurins bind to each other in solution, homophilic teneurin-teneurin binding is unable to support stable cell adhesion, different from heterophilic teneurin-latrophilin binding. Thus, mammalian teneurins act as heterophilic cell-adhesion molecules that may be involved in trans-neuronal interaction processes such as synapse formation or maintenance.

Indexed as

Alternative SplicingAnimalsCell AdhesionDrosophila melanogasterDrosophila ProteinsHEK293 CellsHumansNerve Tissue ProteinsNeuronsProtein BindingRatsReceptors, PeptideSynapsesTenascinalpha-latrotoxin receptorDrosophila ProteinsNerve Tissue ProteinsReceptors, PeptideTenascinAlternative SplicingCell AdhesionFLRT3G Protein-coupled Receptors (GPCR)Ligand-binding ProteinNeurexinNeuronsSynapse FormationTeneurinα-Latrotoxin

Identifiers

PMID24273166
PMCPMC3879561
OpenAlexW1983555571

What OpenQuestion holds

Textmetadata
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.