Evidence map›Paper›PMID 29934346›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2018

PTPσ Drives Excitatory Presynaptic Assembly via Various Extracellular and Intracellular Mechanisms.

Kyung Ah Han, Ji Seung Ko, Gopal Pramanik, Jin Young Kim, Katsuhiko Tabuchi, Ji Won Um, Jaewon Ko

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.9field-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

39 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  4. CASKIN2 mediates PTPσ-orchestrated transsynaptic mechanisms at excitatory synapses.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  6. Review
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  9. Article
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  11. Article
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  14. Cell Adhesion Molecule Signaling at the Synapse: Beyond the Scaffold.Cold Spring Harbor perspectives in biology · 2024
    Review
  15. Article
  16. Molecular definition of distinct active zone protein machineries for CabioRxiv : the preprint server for biology · 2023
    Article
  17. Molecular mechanisms of synaptogenesis.Frontiers in synaptic neuroscience · 2022
    Review
  18. Alterations of presynaptic proteins in autism spectrum disorder.Frontiers in molecular neuroscience · 2022
    Review
  19. Type IIa RPTPs and Glycans: Roles in Axon Regeneration and Synaptogenesis.International journal of molecular sciences · 2021
    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

7 authors at 3 institutions in 2 countries.

Kyung Ah HanDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu 42988, Korea.ORCID 0000-0001-6353-1042
Ji Seung KoDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu 42988, Korea.
Gopal PramanikDepartment of Molecular and Cellular Physiology, Shinshu University School of Medicine, Matsumoto 390-8621, Japan.ORCID 0000-0002-9117-4887
Jin Young KimBiomedical Omics Group, Korea Basic Science Institute, Cheongju, Chungbuk 28119, Korea, and.ORCID 0000-0002-0656-1269
Katsuhiko TabuchiDepartment of Molecular and Cellular Physiology, Shinshu University School of Medicine, Matsumoto 390-8621, Japan.ORCID 0000-0002-1673-4637
Ji Won UmDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu 42988, Korea.ORCID 0000-0002-9355-7726
Jaewon KoDepartment of Brain and Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology, Daegu 42988, Korea, jaewonko@dgist.ac.kr.ORCID 0000-0001-9184-1574
Daegu Gyeongbuk Institute of Science and Technology · KRShinshu University · JPKorea Basic Science Institute · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Leukocyte common antigen-receptor protein tyrosine phosphatases (LAR-RPTPs) are hub proteins that organize excitatory and inhibitory synapse development through binding to various extracellular ligands. Here, we report that knockdown (KD) of the LAR-RPTP family member PTPσ reduced excitatory synapse number and transmission in cultured rat hippocampal neurons, whereas KD of PTPδ produced comparable decreases at inhibitory synapses, in both cases without altering expression levels of interacting proteins. An extensive series of rescue experiments revealed that extracellular interactions of PTPσ with Slitrks are important for excitatory synapse development. These experiments further showed that the intracellular D2 domain of PTPσ is required for induction of heterologous synapse formation by Slitrk1 or TrkC, suggesting that interaction of LAR-RPTPs with distinct intracellular presynaptic proteins, drives presynaptic machinery assembly. Consistent with this, double-KD of liprin-α2 and -α3 or KD of PTPσ substrates (N-cadherin and p250RhoGAP) in neurons inhibited Slitrk6-induced, PTPσ-mediated heterologous synapse formation activity. We propose a synaptogenesis model in presynaptic neurons involving LAR-RPTP-organized retrograde signaling cascades, in which both extracellular and intracellular mechanisms are critical in orchestrating distinct synapse types.

Indexed as

AnimalsHumansNeurogenesisNeuronsRatsReceptor-Like Protein Tyrosine Phosphatases, Class 2Signal TransductionSynapsesSynaptic TransmissionReceptor-Like Protein Tyrosine Phosphatases, Class 2LAR-RPTPspresynaptic assemblyprotein–protein interactionPTPσsynaptic adhesion molecule

Identifiers

PMID29934346
PMCPMC6705959
OpenAlexW2808990236

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.