Evidence map›Paper›PMID 26657011›Full record

ArticleNature communications2015

A CDC42EP4/septin-based perisynaptic glial scaffold facilitates glutamate clearance.

Natsumi Ageta-Ishihara, Maya Yamazaki, Kohtarou Konno, Hisako Nakayama, Manabu Abe, Kenji Hashimoto, Tomoki Nishioka, Kozo Kaibuchi, Satoko Hattori, Tsuyoshi Miyakawa and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. 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
1.0field-weighted citation impact, top 28% 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, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Effects ofFrontiers in molecular neuroscience · 2022
    Article
  10. Article
  11. Article
  12. CDC42 Negatively Regulates Testis-Specific SEPT12 Polymerization.International journal of molecular sciences · 2018
    Article
  13. Article
  14. The Borg family of Cdc42 effector proteins Cdc42EP1-5.Biochemical Society transactions · 2016
    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

17 authors at 7 institutions in 1 country.

Natsumi Ageta-IshiharaDivision of Biological Sciences, Department of Molecular Biology, Nagoya University Graduate School of Science, Nagoya 464-8602, Japan.
Maya YamazakiDepartment of Cellular Neurobiology, Brain Research Institute, Niigata University, Niigata 951-8585, Japan.
Kohtarou KonnoDepartment of Anatomy, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan.
Hisako NakayamaDepartment of Neurophysiology, Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima 734-8551, Japan.
Manabu AbeDepartment of Cellular Neurobiology, Brain Research Institute, Niigata University, Niigata 951-8585, Japan.
Kenji HashimotoDivision of Clinical Neuroscience, Chiba University Center for Forensic Mental Health, Chiba 260-8670, Japan.
Tomoki NishiokaDepartment of Cell Pharmacology, Nagoya University Graduate School of Medicine, Showa, Nagoya 466-8560, Japan.
Kozo KaibuchiDepartment of Cell Pharmacology, Nagoya University Graduate School of Medicine, Showa, Nagoya 466-8560, Japan.
Satoko HattoriDivision of Systems Medical Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake 470-1192, Japan.
Tsuyoshi MiyakawaDivision of Systems Medical Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake 470-1192, Japan.ORCID http://orcid.org/0000-0003-0137-8200
Kohichi TanakaLaboratory of Molecular Neuroscience, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 113-8510, Japan.
Fathul HudaDepartment of Neurophysiology and Neural Repair, Gunma University Graduate School of Medicine, Maebashi, Gunma 371-8511, Japan.
Hirokazu HiraiDepartment of Neurophysiology and Neural Repair, Gunma University Graduate School of Medicine, Maebashi, Gunma 371-8511, Japan.
Kouichi HashimotoDepartment of Neurophysiology, Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima 734-8551, Japan.
Masahiko WatanabeDepartment of Anatomy, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan.
Kenji SakimuraDepartment of Cellular Neurobiology, Brain Research Institute, Niigata University, Niigata 951-8585, Japan.
Makoto KinoshitaDivision of Biological Sciences, Department of Molecular Biology, Nagoya University Graduate School of Science, Nagoya 464-8602, Japan.
Nagoya University · JPHiroshima University · JPNiigata University · JPFujita Health University · JPGunma University · JPHokkaido University · JPTokyo Medical and Dental University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small GTPase-effector proteins CDC42EP1-5/BORG1-5 interact reciprocally with CDC42 or the septin cytoskeleton. Here we show that, in the cerebellum, CDC42EP4 is exclusively expressed in Bergmann glia and localizes beneath specific membrane domains enwrapping dendritic spines of Purkinje cells. CDC42EP4 forms complexes with septin hetero-oligomers, which interact with a subset of glutamate transporter GLAST/EAAT1. In Cdc42ep4(-/-) mice, GLAST is dissociated from septins and is delocalized away from the parallel fibre-Purkinje cell synapses. The excitatory postsynaptic current exhibits a protracted decay time constant, reduced sensitivity to a competitive inhibitor of the AMPA-type glutamate receptors (γDGG) and excessive baseline inward current in response to a subthreshold dose of a nonselective inhibitor of the glutamate transporters/EAAT1-5 (DL-TBOA). Insufficient glutamate-buffering/clearance capacity in these mice manifests as motor coordination/learning defects, which are aggravated with subthreshold DL-TBOA. We propose that the CDC42EP4/septin-based glial scaffold facilitates perisynaptic localization of GLAST and optimizes the efficiency of glutamate-buffering and clearance.

Indexed as

AnimalsCerebellumCytoskeletal ProteinsExcitatory Amino Acid Transporter 1Gene Expression RegulationGlutamic AcidGTPase-Activating ProteinsGTP-Binding Protein RegulatorsMaleMiceMice, KnockoutNeurogliaNeuronsrho GTP-Binding ProteinsRNA-Binding ProteinsSeptinsCDC42EP4 protein, mouseCytoskeletal ProteinsExcitatory Amino Acid Transporter 1Glutamic AcidGTPase-Activating ProteinsGTP-Binding Protein Regulatorsrho GTP-Binding ProteinsRNA-Binding ProteinsSeptinsSlc1a3 protein, mouse

Identifiers

PMID26657011
PMCPMC4682051
OpenAlexW2271681808

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.