Evidence map›Paper›PMID 24145027›Full record

ArticleThe Journal of biological chemistry2013

Presenilins regulate neurotrypsin gene expression and neurotrypsin-dependent agrin cleavage via cyclic AMP response element-binding protein (CREB) modulation.

Angels Almenar-Queralt, Sonia N Kim, Christopher Benner, Cheryl M Herrera, David E Kang, Ivan Garcia-Bassets, Lawrence S B Goldstein

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

10 citing papers in PubMed, 15 citations in OpenAlex.

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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 3 institutions in 1 country.

Angels Almenar-QueraltFrom the Departments of Cellular and Molecular Medicine.
Sonia N Kim
Christopher Benner
Cheryl M Herrera
David E Kang
Ivan Garcia-Bassets
Lawrence S B Goldstein
University of California, San Diego · USSalk Institute for Biological Studies · USSanford Consortium for Regenerative Medicine · US

Funding

VIRUS-INDUCED BRAIN PATHOLOGYP50AG005131 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHUN, JEROLD · 1985 to 2018
$55.4M
Impairment of axonal transport by Amyloid precursor protein and amyloid Beta-protR01AG032180 · NIA · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GOLDSTEIN, LAWRENCE S. · 2007 to 2011
$1.6M
Novel Mechanisms of RanBP9 in APP PathogenesisR01AG033055 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI KANG, DAVID E · 2009 to 2012
$1.2M
Role of Amyloid Precursor Protein in Kinesin TransportF32AG020039 · NIA · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI ALMENAR, ANGELS · 2001 to 2003
$127k
NIA NIH HHS 1F32AG20039NIA NIH HHS 1R01AG033055NIA NIH HHS 5R01AG032180NIA NIH HHS F32 AG020039NIA NIH HHS R01 AG032180NIA NIH HHS R01 AG033055
6 · The paper itself

Abstract

Presenilins, the catalytic components of the γ-secretase complex, are upstream regulators of multiple cellular pathways via regulation of gene transcription. However, the underlying mechanisms and the genes regulated by these pathways are poorly characterized. In this study, we identify Tequila and its mammalian ortholog Prss12 as genes negatively regulated by presenilins in Drosophila larval brains and mouse embryonic fibroblasts, respectively. Prss12 encodes the serine protease neurotrypsin, which cleaves the heparan sulfate proteoglycan agrin. Altered neurotrypsin activity causes serious synaptic and cognitive defects; despite this, the molecular processes regulating neurotrypsin expression and activity are poorly understood. Using γ-secretase drug inhibitors and presenilin mutants in mouse embryonic fibroblasts, we found that a mature γ-secretase complex was required to repress neurotrypsin expression and agrin cleavage. We also determined that PSEN1 endoproteolysis or processing of well known γ-secretase substrates was not essential for this process. At the transcriptional level, PSEN1/2 removal induced cyclic AMP response element-binding protein (CREB)/CREB-binding protein binding, accumulation of activating histone marks at the neurotrypsin promoter, and neurotrypsin transcriptional and functional up-regulation that was dependent on GSK3 activity. Upon PSEN1/2 reintroduction, this active epigenetic state was replaced by a methyl CpG-binding protein 2 (MeCP2)-containing repressive state and reduced neurotrypsin expression. Genome-wide analysis revealed hundreds of other mouse promoters in which CREB binding is similarly modulated by the presence/absence of presenilins. Our study thus identifies Tequila and neurotrypsin as new genes repressed by presenilins and reveals a novel mechanism used by presenilins to modulate CREB signaling based on controlling CREB recruitment.

Indexed as

AgrinAmyloid Precursor Protein SecretasesAnimalsCells, CulturedCyclic AMP Response Element-Binding ProteinDrosophilaDrosophila ProteinsGene Expression RegulationHumansMiceMice, Inbred C57BLMice, TransgenicModels, BiologicalPresenilin-1Presenilin-2Promoter Regions, GeneticAgrinAmyloid Precursor Protein SecretasesCyclic AMP Response Element-Binding ProteinDrosophila ProteinsneurotrypsinPresenilin-1presenilin 1, mousePresenilin-2PSEN1 protein, humanPSEN2 protein, humanPsen2 protein, mouseSerine EndopeptidasesTeq protein, DrosophilaChromatin Immunoprecipitation (ChIP)CREBDrosophila Larval BrainsGSK3MEFsNeurotrypsinPresenilinPromotersSecretasesTequila

Identifiers

PMID24145027
PMCPMC3853272
OpenAlexW2068136170

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.