Evidence map›Paper›PMID 31570833›Full record

ArticleNature cell biology2019

Phagolysosome resolution requires contacts with the endoplasmic reticulum and phosphatidylinositol-4-phosphate signalling.

Roni Levin-Konigsberg, Fernando Montaño-Rendón, Tal Keren-Kaplan, Ren Li, Braeden Ego, Sivakami Mylvaganam, Jessica E DiCiccio, William S Trimble, Michael C Bassik, Juan S Bonifacino and 2 more

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
6.4field-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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.

  1. Stay in touch with the endoplasmic reticulum.Science China. Life sciences · 2024
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Phagocytosis at a glance.Journal of cell science · 2025
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Two-pore channels regulate endomembrane tension to enable remodeling and resolution of phagolysosomes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Review
  18. Article
  19. Article
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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

12 authors at 5 institutions in 2 countries.

Roni Levin-KonigsbergDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.
Fernando Montaño-RendónDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.
Tal Keren-KaplanCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Ren LiDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.
Braeden EgoDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, USA.
Sivakami MylvaganamDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.
Jessica E DiCiccioDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.
William S TrimbleDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0001-9776-5111
Michael C BassikDepartment of Genetics, Stanford University School of Medicine, Stanford, CA, USA.ORCID http://orcid.org/0000-0001-5185-8427
Juan S BonifacinoCell Biology and Neurobiology Branch, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Gregory D FairnDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada. FairnG@smh.ca.ORCID http://orcid.org/0000-0001-6508-168X
Sergio GrinsteinDivision of Cell Biology, Hospital for Sick Children, Toronto, Ontario, Canada. sergio.grinstein@sickkids.ca.ORCID http://orcid.org/0000-0002-0795-4160
University of Toronto · CANational Institutes of Health · USStanford University · USSt. Michael's Hospital · CAHospital for Sick Children · CA

Funding

REGULATION OF THE FATE OF NEWLY SYNTHESIZED PROTEINSZ01HD001607 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BONIFACINO, JUAN · 1991 to 2008
$4.4M
Intramural NIH HHS Z01 HD001607
6 · The paper itself

Abstract

Phosphoinositides have a pivotal role in the maturation of nascent phagosomes into microbicidal phagolysosomes. Following degradation of their contents, mature phagolysosomes undergo resolution, a process that remains largely uninvestigated. Here we studied the role of phosphoinositides in phagolysosome resolution. Phosphatidylinositol-4-phosphate (PtdIns(4)P), which is abundant in maturing phagolysosomes, was depleted as they tubulated and resorbed. Depletion was caused, in part, by transfer of phagolysosomal PtdIns(4)P to the endoplasmic reticulum, a process mediated by oxysterol-binding protein-related protein 1L (ORP1L), a RAB7 effector. ORP1L formed discrete tethers between the phagolysosome and the endoplasmic reticulum, resulting in distinct regions with alternating PtdIns(4)P depletion and enrichment. Tubules emerged from PtdIns(4)P-rich regions, where ADP-ribosylation factor-like protein 8B (ARL8B) and SifA- and kinesin-interacting protein/pleckstrin homology domain-containing family M member 2 (SKIP/PLEKHM2) accumulated. SKIP binds preferentially to monophosphorylated phosphoinositides, of which PtdIns(4)P is most abundant in phagolysosomes, contributing to their tubulation. Accordingly, premature hydrolysis of PtdIns(4)P impaired SKIP recruitment and phagosome resolution. Thus, resolution involves phosphoinositides and tethering of phagolysosomes to the endoplasmic reticulum.

Indexed as

Signal TransductionADP-Ribosylation FactorsAnimalsCRISPR-Cas SystemsEndoplasmic ReticulumGene EditingGene Expression RegulationHumansMiceMonocytesOxysterol Binding ProteinsPhagocytosisPhagosomesPhosphatidylinositol PhosphatesPrimary Cell CultureProteolysisADP-Ribosylation FactorsArl8B protein, mouseOxysterol Binding Proteinsphosphatidylinositol 4-phosphatePhosphatidylinositol Phosphatesrab7 GTP-Binding Proteinsrab7 GTP-binding proteins, humanrab7 GTP-binding proteins, mouserab GTP-Binding ProteinsReceptors, SteroidRNA, Small InterferingVesicular Transport Proteins

Identifiers

PMID31570833
PMCPMC8340083
OpenAlexW2976629614

What OpenQuestion holds

Textmetadata
LicenceTDM
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.