Evidence map›Paper›PMID 25728924›Full record

ArticleStructure (London, England : 1993)2015

Structural basis of latrophilin-FLRT interaction.

Verity A Jackson, Daniel del Toro, Maria Carrasquero, Pietro Roversi, Karl Harlos, Rüdiger Klein, Elena Seiradake

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

51 citing papers in PubMed, 85 citations in OpenAlex.

  1. Adhesion G protein-coupled receptors.Pharmacological reviews · 2026
    Review
  2. Article
  3. Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026
    Review
  4. Review
  5. The far extracellular CUB domain of the adhesion GPCR ADGRG6/GPR126 is a key regulator of receptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 2 institutions in 2 countries.

Verity A JacksonDepartment of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK.
Daniel del ToroMax-Planck Institute of Neurobiology, Am Klopferspitz 18, 82152 Munich-Martinsried, Germany.
Maria CarrasqueroDepartment of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK.
Pietro RoversiDepartment of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK.
Karl HarlosDivision of Structural Biology, Oxford University, Roosevelt Drive, Oxford OX3 7BN, UK.
Rüdiger KleinMax-Planck Institute of Neurobiology, Am Klopferspitz 18, 82152 Munich-Martinsried, Germany; Munich Cluster for Systems Neurology (SyNergy), Feodor-Lynen-Straße 17, 81377 Munich, Germany.
Elena SeiradakeDepartment of Biochemistry, Oxford University, South Parks Road, Oxford OX1 3QU, UK. Electronic address: elena.seiradake@bioch.ox.ac.uk.
University of Oxford · GBMax Planck Institute of Neurobiology · DE

Funding

Medical Research Council G0900084Medical Research Council G1000099Medical Research Council G1100525Medical Research Council MR/L018039/1Medical Research Council MR/M000141/1Medical Research Council MR/N00065X/1Wellcome Trust
6 · The paper itself

Abstract

Latrophilins, receptors for spider venom α-latrotoxin, are adhesion type G-protein-coupled receptors with emerging functions in synapse development. The N-terminal region binds the endogenous cell adhesion molecule FLRT, a major regulator of cortical and synapse development. We present crystallographic data for the mouse Latrophilin3 lectin and olfactomedin-like (Olf) domains, thereby revealing the Olf β-propeller fold and conserved calcium-binding site. We locate the FLRT-Latrophilin binding surfaces by a combination of sequence conservation analysis, point mutagenesis, and surface plasmon resonance experiments. In stripe assays, we show that wild-type Latrophilin3 and its high-affinity interactor FLRT2, but not the binding-impaired mutants we generated, promote HeLa cell adhesion. In contrast, cortical neurons expressing endogenous FLRTs are repelled by wild-type Latrophilin3 and not by the binding-impaired mutant. Taken together, we present molecular level insights into Latrophilin structure, its FLRT-binding mechanism, and a role for Latrophilin and FLRT that goes beyond a simply adhesive interaction.

Indexed as

Amino Acid SequenceAnimalsBinding SitesHEK293 CellsHeLa CellsHumansMembrane GlycoproteinsMiceMolecular Sequence DataProtein BindingReceptors, G-Protein-CoupledReceptors, PeptideAdgrl3 protein, mouseFLRT2 protein, mouseMembrane GlycoproteinsReceptors, G-Protein-CoupledReceptors, Peptide

Identifiers

PMID25728924
PMCPMC4396693
OpenAlexW2138630674

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.