Evidence map›Paper›PMID 27991559›Full record

ArticleScientific reports2016

Shedding of neurexin 3β ectodomain by ADAM10 releases a soluble fragment that affects the development of newborn neurons.

Erika Borcel, Magda Palczynska, Marine Krzisch, Mitko Dimitrov, Giorgio Ulrich, Nicolas Toni, Patrick C Fraering

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. A Bioengineering Strategy to Control ADAM10 Activity in Living Cells.International journal of molecular sciences · 2023
    Article
  7. The Autism Spectrum Disorder-Associated Bacterial MetaboliteInternational journal of molecular sciences · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Proteolytic Processing of Neurexins by Presenilins Sustains Synaptic Vesicle Release.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  15. 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 2 institutions in 1 country.

Erika BorcelBrain Mind Institute and School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH1015 Lausanne, Switzerland.
Magda PalczynskaBrain Mind Institute and School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH1015 Lausanne, Switzerland.
Marine KrzischDepartment of Fundamental Neurosciences, University of Lausanne (UNIL), CH1015 Lausanne, Switzerland.
Mitko DimitrovBrain Mind Institute and School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH1015 Lausanne, Switzerland.
Giorgio UlrichBrain Mind Institute and School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH1015 Lausanne, Switzerland.
Nicolas ToniDepartment of Fundamental Neurosciences, University of Lausanne (UNIL), CH1015 Lausanne, Switzerland.
Patrick C FraeringBrain Mind Institute and School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH1015 Lausanne, Switzerland.
École Polytechnique Fédérale de Lausanne · CHUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurexins are transmembrane synaptic cell adhesion molecules involved in the development and maturation of neuronal synapses. In the present study, we report that Nrxn3β is processed by the metalloproteases ADAM10, ADAM17, and by the intramembrane-cleaving protease γ-secretase, producing secreted neurexin3β (sNrxn3β) and a single intracellular domain (Nrxn3β-ICD). We further completed the full characterization of the sites at which Nrxn3β is processed by these proteases. Supporting the physiological relevance of the Nrxn3β processing, we demonstrate in vivo a significant effect of the secreted shedding product sNrxn3β on the morphological development of adult newborn neurons in the mouse hippocampus. We show that sNrxn3β produced by the cells of the dentate gyrus increases the spine density of newborn neurons whereas sNrxn3β produced by the newborn neuron itself affects the number of its mossy fiber terminal extensions. These results support a pivotal role of sNrxn3β in plasticity and network remodeling during neuronal development.

Indexed as

Protein Processing, Post-TranslationalADAM10 ProteinADAM17 ProteinAmyloid Precursor Protein SecretasesAnimalsAnimals, NewbornHippocampusMembrane ProteinsMice, Inbred C57BLNerve Tissue ProteinsNeuronsProteolysisADAM10 ProteinAdam10 protein, mouseADAM17 ProteinAdam17 protein, mouseAmyloid Precursor Protein SecretasesMembrane ProteinsNerve Tissue Proteinsneurexin 3, mouse

Identifiers

PMID27991559
PMCPMC5171655
OpenAlexW2566478080

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.