Evidence map›Paper›PMID 30760850›Full record

ArticleScientific reports2019

Origin and evolution of plexins, semaphorins, and Met receptor tyrosine kinases.

Chrystian Junqueira Alves, Karla Yotoko, Hongyan Zou, Roland H Friedel

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

36 citing papers in PubMed, 82 citations in OpenAlex.

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  12. Biallelic variants in Plexin B2 (Journal of medical genetics · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Semaphorin signaling restricts neuronal regeneration inFrontiers in cell and developmental biology · 2022
    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

4 authors at 2 institutions in 2 countries.

Chrystian Junqueira AlvesFishberg Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, New York, 10029, USA.ORCID 0000-0003-2224-0729
Karla YotokoBiology Department, Universidade Federal de Viçosa, Viçosa, Minas Gerais, 36570-900, Brazil.ORCID 0000-0003-2051-4204
Hongyan ZouFishberg Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, New York, 10029, USA.ORCID 0000-0003-4216-5607
Roland H FriedelFishberg Department of Neuroscience, Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, New York, 10029, USA. roland.friedel@mssm.edu.ORCID 0000-0002-7513-3604
Allen Institute for Brain Science · USUniversidade Federal de Viçosa · BR

Funding

Plexin-B2 function in glioma invasion and glioma stem cell maintenanceR01NS092735 · NINDS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI FRIEDEL, ROLAND HORST · 2016 to 2025
$4.1M
NINDS NIH HHS R01 NS092735
6 · The paper itself

Abstract

The transition from unicellular to multicellular organisms poses the question as to when genes that regulate cell-cell interactions emerged during evolution. The receptor and ligand pairing of plexins and semaphorins regulates cellular interactions in a wide range of developmental and physiological contexts. We surveyed here genomes of unicellular eukaryotes and of non-bilaterian and bilaterian Metazoa and performed phylogenetic analyses to gain insight into the evolution of plexin and semaphorin families. Remarkably, we detected plexins and semaphorins in unicellular choanoflagellates, indicating their evolutionary origin in a common ancestor of Choanoflagellida and Metazoa. The plexin domain structure is conserved throughout all clades; in contrast, semaphorins are structurally diverse. Choanoflagellate semaphorins are transmembrane proteins with multiple fibronectin type III domains following the N-terminal Sema domain (termed Sema-FN). Other previously not yet described semaphorin classes include semaphorins of Ctenophora with tandem immunoglobulin domains (Sema-IG) and secreted semaphorins of Echinoderamata (Sema-SP, Sema-SI). Our study also identified Met receptor tyrosine kinases (RTKs), which carry a truncated plexin extracellular domain, in several bilaterian clades, indicating evolutionary origin in a common ancestor of Bilateria. In addition, a novel type of Met-like RTK with a complete plexin extracellular domain was detected in Lophotrochozoa and Echinodermata (termed Met-LP RTK). Our findings are consistent with an ancient function of plexins and semaphorins in regulating cytoskeletal dynamics and cell adhesion that predates their role as axon guidance molecules.

Indexed as

Amino Acid SequenceAnimalsBiological EvolutionCell Adhesion MoleculesChoanoflagellataDatabases, GeneticEchinodermataHumansNerve Tissue ProteinsProtein DomainsProto-Oncogene Proteins c-metReceptors, Cell SurfaceSemaphorinsCell Adhesion MoleculesNerve Tissue ProteinsplexinProto-Oncogene Proteins c-metReceptors, Cell SurfaceSemaphorins

Identifiers

PMID30760850
PMCPMC6374515
OpenAlexW2918457706

What OpenQuestion holds

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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.