Evidence map›Paper›PMID 29438049›Full record

ArticleRNA (New York, N.Y.)2018

Oncoprotein AEG-1 is an endoplasmic reticulum RNA-binding protein whose interactome is enriched in organelle resident protein-encoding mRNAs.

Jack C-C Hsu, David W Reid, Alyson M Hoffman, Devanand Sarkar, Christopher V Nicchitta

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

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  10. The Journey of Cancer Cells to the Brain: Challenges and Opportunities.International journal of molecular sciences · 2023
    Review
  11. Article
  12. Article
  13. Regulation and outcomes of localized RNA translation.Wiley interdisciplinary reviews. RNA · 2022
    Review
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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

5 authors at 3 institutions in 1 country.

Jack C-C HsuDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
David W ReidDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
Alyson M HoffmanDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.
Devanand SarkarDepartment of Human and Molecular Genetics, Virginia Commonwealth University Massey Cancer Center, Virginia Commonwealth University Institute of Molecular Medicine, Virginia Commonwealth University School of Medicine, Richmond, Virginia 23298, USA.
Christopher V NicchittaDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.ORCID 0000-0001-7889-1155
Duke Medical Center · USDuke University · USVirginia Commonwealth University · US

Funding

The role of AEG-1 in NASH and NASH-HCCR01DK107451 · NIDDK · VIRGINIA COMMONWEALTH UNIVERSITY · PI SARKAR, DEVANAND · 2016 to 2025
$3.9M
mRNA Localization in Organelle BiogenesisR01GM101533 · NIGMS · DUKE UNIVERSITY · PI NICCHITTA, CHRISTOPHER V. · 2012 to 2020
$2.4M
Mechanisms of Translational Compartmentalization in Eukaryotic CellsR01GM118630 · NIGMS · DUKE UNIVERSITY · PI NICCHITTA, CHRISTOPHER V. · 2017 to 2020
$1.5M
NIDDK NIH HHS R01 DK107451NIGMS NIH HHS R01 GM101533NIGMS NIH HHS R01 GM118630
6 · The paper itself

Abstract

Astrocyte elevated gene-1 (AEG-1), an oncogene whose overexpression promotes tumor cell proliferation, angiogenesis, invasion, and enhanced chemoresistance, is thought to function primarily as a scaffolding protein, regulating PI3K/Akt and Wnt/β-catenin signaling pathways. Here we report that AEG-1 is an endoplasmic reticulum (ER) resident integral membrane RNA-binding protein (RBP). Examination of the AEG-1 RNA interactome by HITS-CLIP and PAR-CLIP methodologies revealed a high enrichment for endomembrane organelle-encoding transcripts, most prominently those encoding ER resident proteins, and within this cohort, for integral membrane protein-encoding RNAs. Cluster mapping of the AEG-1/RNA interaction sites demonstrated a normalized rank order interaction of coding sequence >5' untranslated region, with 3' untranslated region interactions only weakly represented. Intriguingly, AEG-1/membrane protein mRNA interaction sites clustered downstream from encoded transmembrane domains, suggestive of a role in membrane protein biogenesis. Secretory and cytosolic protein-encoding mRNAs were also represented in the AEG-1 RNA interactome, with the latter category notably enriched in genes functioning in mRNA localization, translational regulation, and RNA quality control. Bioinformatic analyses of RNA-binding motifs and predicted secondary structure characteristics indicate that AEG-1 lacks established RNA-binding sites though shares the property of high intrinsic disorder commonly seen in RBPs. These data implicate AEG-1 in the localization and regulation of secretory and membrane protein-encoding mRNAs and provide a framework for understanding AEG-1 function in health and disease.

Indexed as

Cell Adhesion MoleculesEndoplasmic ReticulumHigh-Throughput Nucleotide SequencingHumansIntrinsically Disordered ProteinsMembrane ProteinsOncogene ProteinsRNA-Binding ProteinsRNA, MessengerSequence Analysis, RNACell Adhesion MoleculesIntrinsically Disordered ProteinsMembrane ProteinsMTDH protein, humanOncogene ProteinsRNA-Binding ProteinsRNA, Messengerendoplasmic reticulumRNA-binding proteinRNA localizationsignal sequencetransmembrane protein

Identifiers

PMID29438049
PMCPMC5900566
OpenAlexW2792710786

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.