Evidence map›Paper›PMID 24876378›Full record

ArticleThe Journal of biological chemistry2014

Reelin induces Erk1/2 signaling in cortical neurons through a non-canonical pathway.

Gum Hwa Lee, Zinal Chhangawala, Sventja von Daake, Jeffrey N Savas, John R Yates, Davide Comoletti, Gabriella D'Arcangelo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 59 citations in OpenAlex.

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  6. 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

7 authors at 1 institution in 1 country.

Gum Hwa LeeFrom the Department of Cell Biology and Neuroscience, Rutgers, the State University of New Jersey, Piscataway, New Jersey 08854.
Zinal Chhangawalathe Department of Neuroscience and Cell Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, and.
Sventja von Daakethe Department of Neuroscience and Cell Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, and.
Jeffrey N Savasthe Department of Chemical Physiology and Molecular and Cellular Neurobiology, The Scripps Research Institute, La Jolla, California 92037.
John R Yatesthe Department of Chemical Physiology and Molecular and Cellular Neurobiology, The Scripps Research Institute, La Jolla, California 92037.
Davide Comolettithe Department of Neuroscience and Cell Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, and.
Gabriella D'ArcangeloFrom the Department of Cell Biology and Neuroscience, Rutgers, the State University of New Jersey, Piscataway, New Jersey 08854, darcangelo@biology.rutgers.edu.
Rutgers, The State University of New Jersey · US

Funding

TrainingP41GM103533 · NIGMS · UNIVERSITY OF WASHINGTON · PI MACCOSS, MICHAEL · 2012 to 2021
$20.7M
Caspr2 as an autism candidate gene: a proteomic approach to function & structure.R01MH092906 · NIMH · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI COMOLETTI, DAVIDE · 2011 to 2015
$1.6M
Proteome Biology of Noise Induced Hearing LossK99DC013805 · NIDCD · SCRIPPS RESEARCH INSTITUTE, THE · PI SAVAS, JEFFREY NICHOLAS · 2014 to 2014
$104k
NIDCD NIH HHS K99DC013805-01NIGMS NIH HHS P41 GM103533NIMH NIH HHS R01 MH092906NIMH NIH HHS R01-MH092906
6 · The paper itself

Abstract

Reelin is an extracellular protein that controls many aspects of pre- and postnatal brain development and function. The molecular mechanisms that mediate postnatal activities of Reelin are not well understood. Here, we first set out to express and purify the full length Reelin protein and a biologically active central fragment. Second, we investigated in detail the signal transduction mechanisms elicited by these purified Reelin proteins in cortical neurons. Unexpectedly, we discovered that the full-length Reelin moiety, but not the central fragment, is capable of activating Erk1/2 signaling, leading to increased p90RSK phosphorylation and the induction of immediate-early gene expression. Remarkably, Erk1/2 activation is not mediated by the canonical signal transduction pathway, involving ApoER2/VLDLR and Dab1, that mediates other functions of Reelin in early brain development. The activation of Erk1/2 signaling likely contributes to the modulation of neuronal maturation and synaptic plasticity by Reelin in the postnatal and adult brain.

Indexed as

MAP Kinase Signaling SystemAnimalsCell Adhesion Molecules, NeuronalCerebral CortexExtracellular Matrix ProteinsGene ExpressionGenes, Immediate-EarlyHeterozygoteLDL-Receptor Related ProteinsMiceMice, Inbred ICRMice, KnockoutMice, Neurologic MutantsNerve Tissue ProteinsNeuronsPeptide FragmentsCell Adhesion Molecules, NeuronalDab1 protein, mouseExtracellular Matrix ProteinsLDL-Receptor Related Proteinslow density lipoprotein receptor-related protein 8Nerve Tissue ProteinsPeptide FragmentsProto-Oncogene Proteins c-aktReceptors, LDLReelin ProteinReln protein, mouseRibosomal Protein S6 Kinases, 90-kDaSerine EndopeptidasesVLDL receptorCell CultureCell SignalingExtracellular Signal-regulated Kinase (ERK)NeurodevelopmentSignal Transduction

Identifiers

PMID24876378
PMCPMC4106344
OpenAlexW1972792156

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.