Evidence map›Paper›PMID 21757726›Full record

ArticleThe Journal of biological chemistry2011

Immunity-related GTPase M (IRGM) proteins influence the localization of guanylate-binding protein 2 (GBP2) by modulating macroautophagy.

Maria K Traver, Stanley C Henry, Viviana Cantillana, Tim Oliver, Julia P Hunn, Jonathan C Howard, Sandra Beer, Klaus Pfeffer, Jörn Coers, Gregory A Taylor

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.4field-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

58 citing papers in PubMed, 81 citations in OpenAlex.

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  7. CD47 peptide-cloaked lipid nanoparticles promote cell-specific mRNA delivery.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
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  8. Functional interplay between non-canonical inflammasomes and autophagy in inflammatory responses and diseases.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
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  9. Autophagy and Bacterial infections.Autophagy reports · 2025
    Review
  10. Article
  11. Review
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  13. Steroid treatment suppresses the CD4Scientific reports · 2022
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  14. Review
  15. Immunity-related GTPase IRGM at the intersection of autophagy, inflammation, and tumorigenesis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2022
    Review
  16. Article
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  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

10 authors at 6 institutions in 2 countries.

Maria K TraverDepartment of Molecular Genetics and Microbiology, Duke University, Medical Center, Durham, North Carolina 27710.
Stanley C HenryGeriatric Research, Education, and Clinical Center, VA Medical Center, Durham, North Carolina 27705.
Viviana CantillanaCenter for the Study of Aging and Human Development, Duke University, Medical Center, Durham, North Carolina 27710.
Tim OliverCell Biology, and Medicine, Division of Geriatrics, Duke University, Medical Center, Durham, North Carolina 27710.
Julia P HunnInstitute for Genetics, Department of Cell Genetics, University of Cologne, Cologne 50674, Germany.
Jonathan C HowardInstitute for Genetics, Department of Cell Genetics, University of Cologne, Cologne 50674, Germany.
Sandra BeerInstitute of Medical Microbiology and Hospital Hygiene, Heinrich Heine University of Düsseldorf, Düsseldorf 40225, Germany.
Klaus PfefferInstitute of Medical Microbiology and Hospital Hygiene, Heinrich Heine University of Düsseldorf, Düsseldorf 40225, Germany.
Jörn CoersDepartment of Molecular Genetics and Microbiology, Duke University, Medical Center, Durham, North Carolina 27710.
Gregory A TaylorDepartment of Molecular Genetics and Microbiology, Duke University, Medical Center, Durham, North Carolina 27710; Geriatric Research, Education, and Clinical Center, VA Medical Center, Durham, North Carolina 27705; Center for the Study of Aging and Human Development, Duke University, Medical Center, Durham, North Carolina 27710; Immunology, Duke University, Medical Center, Durham, North Carolina 27710. Electronic address: gregory.taylor@duke.edu.
Duke Medical Center · USDurham VA Medical Center · USHeinrich Heine University Düsseldorf · DEUniversity of Cologne · DEDuke University · USDuke University Hospital · US

Funding

Regulation of IFN-g-induced Innate Immunity by LRG-47R01AI057831 · NIAID · DUKE UNIVERSITY · PI TAYLOR, GREGORY A · 2004 to 2013
$3.1M
NIAID NIH HHS R01 AI057831
6 · The paper itself

Abstract

The immunity-related GTPases (IRGs) are a family of proteins induced by interferon-γ that play a crucial role in innate resistance to intracellular pathogens. The M subfamily of IRG proteins (IRGM) plays a profound role in this context, in part because of the ability of its members to regulate the localization and expression of other IRG proteins. We present here evidence that IRGM proteins affect the localization of the guanylate-binding proteins (GBPs), a second family of interferon-induced GTP-binding proteins that also function in innate immunity. Absence of Irgm1 or Irgm3 led to accumulation of Gbp2 in intracellular compartments that were positive for both the macroautophagy (hereafter referred to as autophagy) marker LC3 and the autophagic adapter molecule p62/Sqstm1. Gbp2 was similarly relocalized in cells in which autophagy was impaired because of the absence of Atg5. Both in Atg5- and IRGM-deficient cells, the IRG protein Irga6 relocalized to the same compartments as Gbp2, raising the possibility of a common regulatory mechanism. However, other data indicated that Irga6, but not Gbp2, was ubiquitinated in IRGM-deficient cells. Similarly, coimmunoprecipitation studies indicated that although Irgm3 did interact directly with Irgb6, it did not interact with Gbp2. Collectively, these data suggest that IRGM proteins indirectly modulate the localization of GBPs through a distinct mechanism from that through which they regulate IRG protein localization. Further, these results suggest that a core function of IRGM proteins is to regulate autophagic flux, which influences the localization of GBPs and possibly other factors that instruct cell-autonomous immune resistance.

Indexed as

AutophagyGene Expression Regulation3T3 CellsAnimalsFlavonolsGlycosidesGTP-Binding ProteinsImmunoprecipitationInterferonsMiceMice, TransgenicModels, BiologicalPhagosomesProtein BindingUbiquitinFlavonolsGbp2 protein, mouseGlycosidesGTP-Binding ProteinsIfi1 protein, mouseInterferonsisorhamnetin 3-O-((S)-3-hydroxy-3-methylglutaroyl(1-6))-alpha-L-rhamnopyranosyl(1-2)-beta-D-glucopyranosideUbiquitin

Identifiers

PMID21757726
PMCPMC3162407
OpenAlexW2161319069

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.