Evidence map›Paper›PMID 30478389›Full record

ArticleNature microbiology2018

An ATG16L1-dependent pathway promotes plasma membrane repair and limits Listeria monocytogenes cell-to-cell spread.

Joel M J Tan, Nora Mellouk, Suzanne E Osborne, Dustin A Ammendolia, Diana N Dyer, Ren Li, Diede Brunen, Jorik M van Rijn, Ju Huang, Mark A Czuczman and 15 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

53 citing papers in PubMed, 72 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

25 authors at 10 institutions in 4 countries.

Joel M J TanCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-6051-3786
Nora MelloukCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0001-8645-6233
Suzanne E OsborneCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Dustin A AmmendoliaCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-7995-5269
Diana N DyerCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Ren LiCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Diede BrunenDepartment of Cell Biology and Institute of Biomembranes, University Medical Center Utrecht, Utrecht, the Netherlands.
Jorik M van RijnDepartment of Cell Biology and Institute of Biomembranes, University Medical Center Utrecht, Utrecht, the Netherlands.
Ju HuangCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Mark A CzuczmanCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Marija A CemmaCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Amy M WonInstitute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario, Canada.
Christopher M YipInstitute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario, Canada.
Ramnik J XavierGastrointestinal Unit and Center for the Study of Inflammatory Bowel Disease, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-5630-5167
Donna A MacDuffDepartment of Microbiology and Immunology, University of Illinois at Chicago College of Medicine, Chicago, IL, USA.
Fulvio ReggioriDepartment of Cell Biology and Institute of Biomembranes, University Medical Center Utrecht, Utrecht, the Netherlands.
Jayanta DebnathDepartment of Pathology and Helen Diller Family Comprehensive Cancer Center, University of California, San Francisco, San Francisco, CA, USA.
Tamotsu YoshimoriDepartment of Cellular Regulation and Host Defense, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan.
Peter K KimCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.
Gregory D FairnDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Etienne CoyaudPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario, Canada.
Brian RaughtPrincess Margaret Cancer Centre, University Health Network, Toronto, Ontario, Canada.
Aleixo M MuiseCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0001-9624-3346
Darren E HigginsDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, USA.
John H BrumellCell Biology Program, Hospital for Sick Children, Toronto, Ontario, Canada. john.brumell@sickkids.ca.ORCID http://orcid.org/0000-0002-5802-7789
University of Toronto · CAHospital for Sick Children · CAHarvard University · USUniversity Health Network · CAUniversity Medical Center Utrecht · NLSt. Michael's Hospital · CAThe University of Osaka · JPUniversity Medical Center Groningen · NLUniversity of California, San Francisco · USUniversity of Illinois Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasma membrane integrity is essential for the viability of eukaryotic cells. In response to bacterial pore-forming toxins, disrupted regions of the membrane are rapidly repaired. However, the pathways that mediate plasma membrane repair are unclear. Here we show that autophagy-related (ATG) protein ATG16L1 and its binding partners ATG5 and ATG12 are required for plasma membrane repair through a pathway independent of macroautophagy. ATG16L1 is required for lysosome fusion with the plasma membrane and blebbing responses that promote membrane repair. ATG16L1 deficiency causes accumulation of cholesterol in lysosomes that contributes to defective membrane repair. Cell-to-cell spread by Listeria monocytogenes requires membrane damage by the bacterial toxin listeriolysin O, which is restricted by ATG16L1-dependent membrane repair. Cells harbouring the ATG16L1 T300A allele associated with inflammatory bowel disease were also found to accumulate cholesterol and be defective in repair, linking a common inflammatory disease to plasma membrane integrity. Thus, plasma membrane repair could be an important therapeutic target for the treatment of bacterial infections and inflammatory disorders.

Indexed as

AnimalsAutophagyAutophagy-Related Protein 12Autophagy-Related Protein 5Autophagy-Related ProteinsBacterial ToxinsCarrier ProteinsCell MembraneCholesterolDisease Models, AnimalExocytosisHeat-Shock ProteinsHeLa CellsHemolysin ProteinsHumansListeria monocytogenesATG12 protein, humanATG16L1 protein, humanAtg16l1 protein, mouseATG5 protein, humanAutophagy-Related Protein 12Autophagy-Related Protein 5Autophagy-Related ProteinsBacterial ToxinsCarrier ProteinsCholesterolHeat-Shock ProteinsHemolysin ProteinshlyA protein, Listeria monocytogenes

Identifiers

PMID30478389
OpenAlexW2901854852

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.