Evidence map›Paper›PMID 27480238›Full record

ArticleNature communications2016

SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion.

Eunkyung Lie, Ji Seung Ko, Su-Yeon Choi, Junyeop Daniel Roh, Yi Sul Cho, Ran Noh, Doyoun Kim, Yan Li, Hyeyeon Kang, Tae-Yong Choi and 12 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. 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
3.0field-weighted citation impact, top 9% 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, 33 citations in OpenAlex.

  1. Significance ofFrontiers in pharmacology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain.Frontiers in cell and developmental biology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. SALM4 regulates angiogenic functions in endothelial cells through VEGFR2 phosphorylation at Tyr1175.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. SALM/Lrfn Family Synaptic Adhesion Molecules.Frontiers in molecular neuroscience · 2018
    Review
  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

22 authors at 6 institutions in 3 countries.

Eunkyung LieDepartment of Biological Sciences, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea.
Ji Seung KoDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Su-Yeon ChoiCenter for Synaptic Brain Dysfunctions, Institute for Basic Science, Daejeon 305-701, Korea.
Junyeop Daniel RohCenter for Synaptic Brain Dysfunctions, Institute for Basic Science, Daejeon 305-701, Korea.
Yi Sul ChoDepartment of Anatomy and Neurobiology, School of Dentistry, Kyungpook National University, Daegu 700-412, Korea.
Ran NohCenter for Cognition and Sociality, Institute for Basic Science, Daejeon 305-701, Korea.
Doyoun KimCenter for Synaptic Brain Dysfunctions, Institute for Basic Science, Daejeon 305-701, Korea.
Yan LiCenter for Synaptic Brain Dysfunctions, Institute for Basic Science, Daejeon 305-701, Korea.
Hyeyeon KangDepartment of Physiology and BK21 PLUS Project to Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Tae-Yong ChoiDepartment of Physiology, Seoul National University School of Dentistry, Seoul 110-749, Korea.
Jungyong NamDepartment of Biological Sciences, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea.
Won MahDepartment of Anatomy and Neurobiology, School of Dentistry, Kyungpook National University, Daegu 700-412, Korea.
Dongmin LeeDepartment of Anatomy and Division of Brain Korea 21, Biomedical Science, College of Medicine, Korea University, Seoul 136-705, Korea.
Seong-Gyu LeeGraduate School of Medical Science and Engineering, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea.
Ho Min KimGraduate School of Medical Science and Engineering, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea.
Hyun KimDepartment of Anatomy and Division of Brain Korea 21, Biomedical Science, College of Medicine, Korea University, Seoul 136-705, Korea.
Se-Young ChoiDepartment of Physiology, Seoul National University School of Dentistry, Seoul 110-749, Korea.ORCID 0000-0001-7534-5167
Ji Won UmDepartment of Physiology and BK21 PLUS Project to Medical Sciences, Yonsei University College of Medicine, Seoul 120-752, Korea.
Myoung-Goo KangCenter for Cognition and Sociality, Institute for Basic Science, Daejeon 305-701, Korea.
Yong Chul BaeDepartment of Anatomy and Neurobiology, School of Dentistry, Kyungpook National University, Daegu 700-412, Korea.
Jaewon KoDepartment of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 120-749, Korea.
Eunjoon KimDepartment of Biological Sciences, Korea Advanced Institute for Science and Technology, Daejeon 305-701, Korea.
Korea Advanced Institute of Science and Technology · KRInstitute for Basic Science · KRYonsei University · KRKyungpook National University · KRSeoul National University · KRKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synaptic adhesion molecules regulate various aspects of synapse development, function and plasticity. These functions mainly involve trans-synaptic interactions and positive regulations, whereas cis-interactions and negative regulation are less understood. Here we report that SALM4, a member of the SALM/Lrfn family of synaptic adhesion molecules, suppresses excitatory synapse development through cis inhibition of SALM3, another SALM family protein with synaptogenic activity. Salm4-mutant (Salm4(-/-)) mice show increased excitatory synapse numbers in the hippocampus. SALM4 cis-interacts with SALM3, inhibits trans-synaptic SALM3 interaction with presynaptic LAR family receptor tyrosine phosphatases and suppresses SALM3-dependent presynaptic differentiation. Importantly, deletion of Salm3 in Salm4(-/-) mice (Salm3(-/-); Salm4(-/-)) normalizes the increased excitatory synapse number. These results suggest that SALM4 negatively regulates excitatory synapses via cis inhibition of the trans-synaptic SALM3-LAR adhesion.

Indexed as

AnimalsCA1 Region, HippocampalCell AdhesionCell Adhesion Molecules, NeuronalCell DifferentiationExcitatory Postsynaptic PotentialsFemaleMaleMembrane GlycoproteinsMiceMice, Inbred C57BLMice, KnockoutModels, AnimalNerve Tissue ProteinsNeural Cell Adhesion MoleculesPresynaptic TerminalsCell Adhesion Molecules, NeuronalLrfn3 protein, mouseLrfn4 protein, mouseMembrane GlycoproteinsNerve Tissue ProteinsNeural Cell Adhesion MoleculesReceptor-Like Protein Tyrosine Phosphatases, Class 2

Identifiers

PMID27480238
PMCPMC4974644
OpenAlexW2502560377

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.