Evidence map›Paper›PMID 33140520›Full record

ArticleEMBO reports2020

Inositol-requiring enzyme-1 regulates phosphoinositide signaling lipids and macrophage growth.

Syed Muhammad Hamid, Mevlut Citir, Erdem Murat Terzi, Ismail Cimen, Zehra Yildirim, Asli Ekin Dogan, Begum Kocaturk, Umut Inci Onat, Moshe Arditi, Christian Weber and 3 more

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

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  13. Regulation of lipid metabolism by the unfolded protein response.Journal of cellular and molecular medicine · 2021
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 8 institutions in 4 countries.

Syed Muhammad HamidSmidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA.
Mevlut CitirThe Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Erdem Murat TerziDepartment of Pathology, Laura & Isaac Perlmutter Cancer Center, New York University School of Medicine, New York, NY, USA.
Ismail CimenInstitute for Cardiovascular Prevention, LMU Munich, German Cardiovascular Research Centre, partner site Munich Heart Alliance Munich, Munich, Germany.ORCID 0000-0002-8182-6968
Zehra YildirimSmidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA.
Asli Ekin DoganSmidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA.
Begum KocaturkDepartment of Pediatrics and Medicine, Division of Infectious Diseases and Immunology, and Infectious and Immunologic Diseases Research Center, Department of Biomedical Sciences, Cedars-Sinai Medical Center, Los Angeles, CA, USA.ORCID 0000-0003-3657-6055
Umut Inci OnatDepartment of Molecular Biology and Genetics, Bilkent University, Ankara, Turkey.
Moshe ArditiSmidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA.
Christian WeberInstitute for Cardiovascular Prevention, LMU Munich, German Cardiovascular Research Centre, partner site Munich Heart Alliance Munich, Munich, Germany.ORCID 0000-0003-4610-8714
Alexis Traynor-KaplanDepartment of Medicine, University of Washington School of Medicine, Seattle, WA, USA.
Carsten SchultzThe Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.ORCID 0000-0002-5824-2171
Ebru ErbaySmidt Heart Institute, Cedars-Sinai Medical Center, Los Angeles, CA, USA.ORCID 0000-0001-9584-1803
Cedars-Sinai Medical Center · USBilkent University · TREuropean Molecular Biology Laboratory · DEGerman Centre for Cardiovascular Research · DEMaastricht University · NLNew York University · USOregon Health & Science University · USUniversity of Washington · US

Funding

Deutsche Forschungsgemeinschaft (DFG) DFG Transregio 83Deutsche Forschungsgemeinschaft (DFG) DFG Transregio 86Deutsche Forschungsgemeinschaft (DFG) SFB 1123Deutsche Forschungsgemeinschaft (DFG) TRR 267-A02FP7 Ideas: European Research Council (FP7 Ideas) 336643FP7 Ideas: European Research Council (FP7 Ideas) 692511Fulbright Association (FULBRIGHT) FY-2017-TR-PD-01
6 · The paper itself

Abstract

The ER-bound kinase/endoribonuclease (RNase), inositol-requiring enzyme-1 (IRE1), regulates the phylogenetically most conserved arm of the unfolded protein response (UPR). However, the complex biology and pathology regulated by mammalian IRE1 cannot be fully explained by IRE1's one known, specific RNA target, X box-binding protein-1 (XBP1) or the RNA substrates of IRE1-dependent RNA degradation (RIDD) activity. Investigating other specific substrates of IRE1 kinase and RNase activities may illuminate how it performs these diverse functions in mammalian cells. We report that macrophage IRE1 plays an unprecedented role in regulating phosphatidylinositide-derived signaling lipid metabolites and has profound impact on the downstream signaling mediated by the mammalian target of rapamycin (mTOR). This cross-talk between UPR and mTOR pathways occurs through the unconventional maturation of microRNA (miR) 2137 by IRE1's RNase activity. Furthermore, phosphatidylinositol (3,4,5) phosphate (PI(3,4,5)P

Indexed as

Endoplasmic Reticulum StressPhosphatidylinositolsEndoribonucleasesHumansInositolMacrophagesProtein Serine-Threonine KinasesUnfolded Protein ResponseEndoribonucleasesERN1 protein, humanInositolPhosphatidylinositolsProtein Serine-Threonine KinasesER stresshyperlipidemiamacrophagemicroRNAmTOR signaling

Identifiers

PMID33140520
PMCPMC7726810
OpenAlexW3095319430

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.