Evidence map›Paper›PMID 36929840›Full record

ArticleG3 (Bethesda, Md.)2023

The human RAP1 and GFAPɛ proteins increase γ-secretase activity in a yeast model system.

Mark J Swanson, Kelsey N Lewis, Robert Carpenter, Alexis Whetzel, Nancy S Bae

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

5 authors at 1 institution in 1 country.

Mark J SwansonDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ 85308, USA.
Kelsey N LewisDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ 85308, USA.
Robert CarpenterDepartment of Biomedical Sciences, College of Graduate Studies, Midwestern University, Glendale, AZ 85308, USA.
Alexis WhetzelDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ 85308, USA.
Nancy S BaeDepartment of Biochemistry and Molecular Genetics, Midwestern University, Glendale, AZ 85308, USA.
Midwestern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is an age-related disorder that results in progressive cognitive impairment and memory loss. Deposition of amyloid β (Aβ) peptides in senile plaques is a hallmark of AD. γ-secretase produces Aβ peptides, mostly as the soluble Aβ40 with fewer insoluble Aβ42 peptides. Rare, early-onset AD (EOAD) occurs in individuals under 60 years of age. Most EOAD cases are due to unknown genetic causes, but a subset is due to mutations in the genes encoding the amyloid precursor protein that is processed into Aβ peptides or the presenilins (PS1 and PS2) that process APP. PS1 interacts with the epsilon isoform of glial fibrillary acidic protein (GFAPɛ), a protein found in the subventricular zone of the brain. We have found that GFAPɛ interacts with the telomere protection factor RAP1 (TERF2IP). RAP1 can also interact with PS1 alone or with GFAPɛ in vitro. Our data show that the nuclear protein RAP1 has an extratelomeric role in the cytoplasm through its interactions with GFAPɛ and PS1. GFAPɛ coprecipitated with RAP1 from human cell extracts. RAP1, GFAPɛ, and PS1 all colocalized in human SH-SY5Y cells. Using a genetic model of the γ-secretase complex in Saccharomyces cerevisiae, RAP1 increased γ-secretase activity, and this was potentiated by GFAPɛ. Our studies are the first to connect RAP1 with an age-related disorder.

Indexed as

Alzheimer DiseaseNeuroblastomaSaccharomyces cerevisiae ProteinsAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesGlial Fibrillary Acidic ProteinHumansSaccharomyces cerevisiaeShelterin ComplexTelomere-Binding ProteinsTranscription FactorsAmyloid beta-PeptidesAmyloid Precursor Protein SecretasesGlial Fibrillary Acidic ProteinRAP1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsShelterin ComplexTelomere-Binding ProteinsTERF2IP protein, humanTranscription FactorsAlzheimer's diseaseamyloid betaGFAPɛRAP1Saccharomyces cerevisiaeTERF2IPγ-secretase

Identifiers

PMID36929840
PMCPMC10411568
OpenAlexW4327684367

What Socratic holds

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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 Socratic graph.