Evidence map›Paper›PMID 31417095›Full record

ArticleNature communications2019

Diversity of oligomerization in Drosophila semaphorins suggests a mechanism of functional fine-tuning.

Daniel Rozbesky, Ross A Robinson, Vitul Jain, Max Renner, Tomas Malinauskas, Karl Harlos, Christian Siebold, E Yvonne Jones

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Molecular mechanisms of proteoglycan-mediated semaphorin signaling in axon guidance.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  6. Review
  7. Identifying Function Determining Residues in Neuroimmune Semaphorin 4A.International journal of molecular sciences · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. The Role of Semaphorins in Metabolic Disorders.International journal of molecular sciences · 2020
    Review
  12. Article
  13. Article
  14. Review
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

8 authors at 1 institution in 1 country.

Daniel RozbeskyDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK. daniel@strubi.ox.ac.uk.ORCID http://orcid.org/0000-0001-6546-8219
Ross A RobinsonDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.
Vitul JainDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.ORCID http://orcid.org/0000-0002-8396-8329
Max RennerDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.
Tomas MalinauskasDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.ORCID http://orcid.org/0000-0002-4847-5529
Karl HarlosDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.ORCID http://orcid.org/0000-0002-7266-4354
Christian SieboldDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK.ORCID http://orcid.org/0000-0002-6635-3621
E Yvonne JonesDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, OX3 7BN, UK. yvonne@strubi.ox.ac.uk.ORCID http://orcid.org/0000-0002-3834-1893
Centre for Human Genetics · GB

Funding

Cancer Research UK 17721Cancer Research UK 26752Cancer Research UK C20724/A14414Cancer Research UK C20724/A26752Cancer Research UK C375/A17721Medical Research Council MR/L017776/1Medical Research Council MR/M000141/1Wellcome Trust 203141/Z/16/ZWellcome Trust 204703/Z/16/Z
6 · The paper itself

Abstract

Semaphorin ligands and their plexin receptors are one of the major cell guidance factors that trigger localised changes in the cytoskeleton. Binding of semaphorin homodimer to plexin brings two plexins in close proximity which is a prerequisite for plexin signalling. This model appears to be too simplistic to explain the complexity and functional versatility of these molecules. Here, we determine crystal structures for all members of Drosophila class 1 and 2 semaphorins. Unlike previously reported semaphorin structures, Sema1a, Sema2a and Sema2b show stabilisation of sema domain dimer formation via a disulfide bond. Unexpectedly, our structural and biophysical data show Sema1b is a monomer suggesting that semaphorin function may not be restricted to dimers. We demonstrate that semaphorins can form heterodimers with members of the same semaphorin class. This heterodimerization provides a potential mechanism for cross-talk between different plexins and co-receptors to allow fine-tuning of cell signalling.

Indexed as

AnimalsCrystallography, X-RayDimerizationDrosophila melanogasterDrosophila ProteinsModels, MolecularMolecular Dynamics SimulationNerve Tissue ProteinsPolymerizationReceptors, Cell SurfaceSemaphorinsDrosophila ProteinsNerve Tissue ProteinsplexA protein, DrosophilaplexB protein, DrosophilaReceptors, Cell Surfacesemaphorin 1a, DrosophilaSemaphorins

Identifiers

PMID31417095
PMCPMC6695400
OpenAlexW2964608088

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.