Evidence map›Paper›PMID 33009002›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2020

Reelin-Nrp1 Interaction Regulates Neocortical Dendrite Development in a Context-Specific Manner.

Takao Kohno, Keisuke Ishii, Yuki Hirota, Takao Honda, Makoto Makino, Takahiko Kawasaki, Kazunori Nakajima, Mitsuharu Hattori

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2020. 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
1.4field-weighted citation impact, top 22% 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, 26 citations in OpenAlex.

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  5. Beyond Glycolysis: Aldolase A Is a Novel Effector in Reelin-Mediated Dendritic Development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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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

8 authors at 3 institutions in 1 country.

Takao KohnoDepartment of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-8603, Japan tkohno@phar.nagoya-cu.ac.jp mhattori@phar.nagoya-cu.ac.jp.ORCID 0000-0003-2557-4281
Keisuke IshiiDepartment of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-8603, Japan.
Yuki HirotaDepartment of Anatomy, Keio University School of Medicine, Tokyo, 160-8582, Japan.
Takao HondaDepartment of Anatomy, Keio University School of Medicine, Tokyo, 160-8582, Japan.
Makoto MakinoDepartment of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-8603, Japan.
Takahiko KawasakiBrain Function Laboratory, National Institute of Genetics, Mishima, Shizuoka 411-8540, Japan.
Kazunori NakajimaDepartment of Anatomy, Keio University School of Medicine, Tokyo, 160-8582, Japan.ORCID 0000-0003-1864-9425
Mitsuharu HattoriDepartment of Biomedical Science, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya, Aichi 467-8603, Japan tkohno@phar.nagoya-cu.ac.jp mhattori@phar.nagoya-cu.ac.jp.ORCID 0000-0002-0503-4969
Nagoya City University · JPKeio University · JPNational Institute of Genetics · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reelin plays versatile roles in neocortical development. The C-terminal region (CTR) of Reelin is required for the correct formation of the superficial structure of the neocortex; however, the mechanisms by which this position-specific effect occurs remain largely unknown. In this study, we demonstrate that Reelin with an intact CTR binds to neuropilin-1 (Nrp1), a transmembrane protein. Both male and female mice were used. Nrp1 is localized with very-low-density lipoprotein receptor (VLDLR), a canonical Reelin receptor, in the superficial layers of the developing neocortex. It forms a complex with VLDLR, and this interaction is modulated by the alternative splicing of VLDLR. Reelin with an intact CTR binds more strongly to the VLDLR/Nrp1 complex than to VLDLR alone. Knockdown of Nrp1 in neurons leads to the accumulation of Dab1 protein. Since the degradation of Dab1 is induced by Reelin signaling, it is suggested that Nrp1 augments Reelin signaling. The interaction between Reelin and Nrp1 is required for normal dendritic development in superficial-layer neurons. All of these characteristics of Reelin are abrogated by proteolytic processing of the six C-terminal amino acid residues of Reelin (0.17% of the whole protein). Therefore, Nrp1 is a coreceptor molecule for Reelin and, together with the proteolytic processing of Reelin, can account for context-specific Reelin function in brain development.

Indexed as

AnimalsCell Adhesion Molecules, NeuronalCell LineDendritesDNAExtracellular Matrix ProteinsFemaleGene Knockdown TechniquesMaleMiceMice, Inbred ICRNeocortexNerve Tissue ProteinsNeuropilin-1Receptors, LDLReelin ProteinCell Adhesion Molecules, NeuronalDab1 protein, mouseDNAExtracellular Matrix ProteinsNerve Tissue ProteinsNeuropilin-1Receptors, LDLReelin ProteinReln protein, mouseSerine EndopeptidasesVLDL receptordendriteneocortexneuropilinproteolysisradial migration

Identifiers

PMID33009002
PMCPMC7577592
OpenAlexW3091003608

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.