Evidence map›Paper›PMID 27172324›Full record

ArticleAutophagy2016

Targeting by AutophaGy proteins (TAG): Targeting of IFNG-inducible GTPases to membranes by the LC3 conjugation system of autophagy.

Sungwoo Park, Jayoung Choi, Scott B Biering, Erin Dominici, Lelia E Williams, Seungmin Hwang

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
8.3field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Guideline
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  7. Animal venoms: a novel source of anti-Frontiers in pharmacology · 2023
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  10. Unlocking the gate to GABARAPL2.Biologia futura · 2022
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  12. Host autophagy limitsFrontiers in microbiology · 2022
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  13. The role of SIRT1 in the process ofFrontiers in microbiology · 2022
    Article
  14. Review
  15. Article
  16. Cell-autonomousLife science alliance · 2021
    Article
  17. Review
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Sungwoo Parka Department of Pathology , University of Chicago , Chicago , IL , USA.
Jayoung Choia Department of Pathology , University of Chicago , Chicago , IL , USA.
Scott B Bieringb Committee on Microbiology, University of Chicago , Chicago , IL , USA.
Erin Dominicia Department of Pathology , University of Chicago , Chicago , IL , USA.
Lelia E Williamsa Department of Pathology , University of Chicago , Chicago , IL , USA.
Seungmin Hwanga Department of Pathology , University of Chicago , Chicago , IL , USA.
University of Chicago · US

Funding

VIRAL ONCOLOGY CORE FACILITYP30CA014599 · NCI · UNIVERSITY OF CHICAGO · PI MARK W. LINGEN · 1985 to 2026
$122.1M
ULTRASTRUCTURE AND CYTOMORPHOLOGY COREP30DK042086 · NIDDK · UNIVERSITY OF CHICAGO · PI LIU, CAMBRIAN YANGSHAO · 1990 to 2025
$29.8M
Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
NCI NIH HHS P30 CA014599NIDDK NIH HHS P30 DK042086NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

LC3 has been used as a marker to locate autophagosomes. However, it is also well established that LC3 can localize on various membranous structures other than autophagosomes. We recently demonstrated that the LC3 conjugation system (ATG7, ATG3, and ATG12-ATG5-ATG16L1) is required to target LC3 and IFNG (interferon, gamma)-inducible GTPases to the parasitophorus vacuole membrane (PVM) of a protist parasite Toxoplasma gondii and consequently for IFNG to control T. gondii infection. Here we show that not only LC3, but also its homologs (GABARAP, GABARAPL1, and GABARAPL2) localize on the PVM of T. gondii in a conjugation-dependent manner. Knockout/knockdown of all LC3 homologs led to a significant reduction in targeting of the IFNG-inducible GTPases to the PVM of T. gondii and the IFNG-mediated control of T. gondii infection. Furthermore, when we relocated the ATG12-ATG5-ATG16L1 complex, which specifies the conjugation site of LC3 homologs, to alternative target membranes, the IFNG-inducible GTPases were targeted to the new target membranes rather than the PVM of T. gondii. These data suggest that the localization of LC3 homologs onto a membrane by the LC3 conjugation system is necessary and sufficient for targeting of the IFNG-inducible GTPases to the membrane, implying Targeting by AutophaGy proteins (TAG). Our data further suggest that the conjugation of ubiquitin-like LC3 homologs to the phospholipids of membranes may change the destiny of the membranes beyond degradation through lysosomal fusion, as the conjugation of ubiquitin to proteins changes the destiny of the proteins beyond proteasomal degradation.

Indexed as

AnimalsAutophagyAutophagy-Related ProteinsCells, CulturedGTP PhosphohydrolasesInterferon-gammaMiceMicrotubule-Associated ProteinsToxoplasmaUbiquitin-Conjugating EnzymesAutophagy-Related ProteinsGTP PhosphohydrolasesIFNG protein, mouseInterferon-gammaMap1lc3b protein, mouseMicrotubule-Associated ProteinsUbiquitin-Conjugating EnzymesautophagyGBPIFNIRGLC3TAGtargetingToxoplasma gondiiubiquitin

Identifiers

PMID27172324
PMCPMC4990996
OpenAlexW2364884796

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.