Evidence map›Paper›PMID 29317426›Full record

ArticleThe EMBO journal2018

The WD40 domain of ATG16L1 is required for its non-canonical role in lipidation of LC3 at single membranes.

Katherine Fletcher, Rachel Ulferts, Elise Jacquin, Talitha Veith, Noor Gammoh, Julia M Arasteh, Ulrike Mayer, Simon R Carding, Thomas Wileman, Rupert Beale and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 185 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
185citing papers in PubMed, 3 pooled it
12.2field-weighted citation impact, top 1% 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

185 citing papers in PubMed, 3 syntheses or guidelines pooled it, 288 citations in OpenAlex.

  1. Pooled it
  2. Guideline
  3. Investigation ofMedicina (Kaunas, Lithuania) · 2019
    Pooled it
  4. Review
  5. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
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125 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 1 country.

Katherine FletcherSignalling Programme, Babraham Institute, Cambridge, UK.
Rachel UlfertsDivision of Virology, Department of Pathology, University of Cambridge, Cambridge, UK.
Elise JacquinSignalling Programme, Babraham Institute, Cambridge, UK.
Talitha VeithDivision of Virology, Department of Pathology, University of Cambridge, Cambridge, UK.
Noor GammohEdinburgh Cancer Research UK Centre University of Edinburgh, Edinburgh, UK.
Julia M ArastehNorwich Medical School, UEA, Norwich, UK.
Ulrike MayerSchool of Biological Sciences, UEA, Norwich, UK.
Simon R CardingQuadrum Institute Bioscience, Norwich Research Park, Norwich, UK.ORCID 0000-0002-2383-9701
Thomas WilemanNorwich Medical School, UEA, Norwich, UK.
Rupert BealeDivision of Virology, Department of Pathology, University of Cambridge, Cambridge, UK rclb2@cam.ac.uk Oliver.Florey@babraham.ac.uk.ORCID 0000-0002-6705-8560
Oliver FloreySignalling Programme, Babraham Institute, Cambridge, UK rclb2@cam.ac.uk Oliver.Florey@babraham.ac.uk.ORCID 0000-0002-1075-7424
Babraham Institute · GBUniversity of Cambridge · GBEdinburgh Cancer Research · GBNorwich Research Park · GBUniversity of East Anglia · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004529/1Biotechnology and Biological Sciences Research Council BBS/E/F/000PR10353Biotechnology and Biological Sciences Research Council BBS/E/F/000PR10355Cancer Research UK 16337Cancer Research UK C47718/A16337Medical Research Council MR/M00869X/1Medical Research Council RG89611
6 · The paper itself

Abstract

A hallmark of macroautophagy is the covalent lipidation of LC3 and insertion into the double-membrane phagophore, which is driven by the ATG16L1/ATG5-ATG12 complex. In contrast, non-canonical autophagy is a pathway through which LC3 is lipidated and inserted into single membranes, particularly endolysosomal vacuoles during cell engulfment events such as LC3-associated phagocytosis. Factors controlling the targeting of ATG16L1 to phagophores are dispensable for non-canonical autophagy, for which the mechanism of ATG16L1 recruitment is unknown. Here we show that the WD repeat-containing C-terminal domain (WD40 CTD) of ATG16L1 is essential for LC3 recruitment to endolysosomal membranes during non-canonical autophagy, but dispensable for canonical autophagy. Using this strategy to inhibit non-canonical autophagy specifically, we show a reduction of MHC class II antigen presentation in dendritic cells from mice lacking the WD40 CTD Further, we demonstrate activation of non-canonical autophagy dependent on the WD40 CTD during influenza A virus infection. This suggests dependence on WD40 CTD distinguishes between macroautophagy and non-canonical use of autophagy machinery.

Indexed as

AutophagyWD40 RepeatsAnimalsAntigen PresentationAutophagy-Related ProteinsCarrier ProteinsCells, CulturedClass III Phosphatidylinositol 3-KinasesDendritic CellsEndosomesFemaleHumansInfluenza A virusInfluenza, HumanIntracellular MembranesLysosomesATG16L1 protein, humanAtg16l1 protein, mouseAutophagy-Related ProteinsCarrier ProteinsClass III Phosphatidylinositol 3-KinasesMAP1LC3A protein, humanMembrane LipidsMicrotubule-Associated ProteinsATG16L1autophagyinfluenzaLC3phagocytosis

Identifiers

PMID29317426
PMCPMC5813257
OpenAlexW2782659115

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.