Evidence map›Paper›PMID 40983659›Full record

ArticleNature cell biology2025

Membrane receptors cluster phosphatidylserine to activate LC3-associated phagocytosis.

Emilio Boada-Romero, Clifford S Guy, Gustavo Palacios, Luigi Mari, Suresh Poudel, Zhenrui Li, Piyush Sharma, Douglas R Green

Abstract read
In one paragraph

Article in Nature cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Bon appétit, your phagocyte.Cell death discovery · 2026
    Review
  7. Article
  8. Article
  9. Review
  10. 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

8 authors.

Emilio Boada-RomeroDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA. emilio.boadaromero@stjude.org.ORCID http://orcid.org/0000-0003-2482-076X
Clifford S GuyDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Gustavo PalaciosDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0009-0001-2483-3774
Luigi MariDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0002-2903-7689
Suresh PoudelDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Zhenrui LiDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Piyush SharmaDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0003-1185-9534
Douglas R GreenDepartment of Immunology, St. Jude Children's Research Hospital, Memphis, TN, USA. douglas.green@stjude.org.ORCID http://orcid.org/0000-0002-7332-1417

Funding

MECHANISMS OF REGULATED CELL DEATHR35CA231620 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI Douglas R. Green · 2018 to 2026
$9.2M
NCI NIH HHS R35 CA231620U.S. Department of Health & Human Services | National Institutes of Health (NIH) R35CA231620
6 · The paper itself

Abstract

LC3-associated phagocytosis (LAP) represents a non-canonical function of autophagy proteins in which ATG8-family proteins (LC3 and GABARAP proteins) are lipidated onto single-membrane phagosomes as particles are engulfed by phagocytic cells. LAP plays roles in innate immunity, inflammation and anticancer responses, and is initiated following phagocytosis of particles that stimulate Toll-like receptors (TLR) and Fc receptors as well as following engulfment of dying cells. However, how this molecular process is initiated remains elusive. Here we report that receptors that engage LAP enrich phosphatidylserine (PS) in the phagosome membrane via membrane-proximal domains that are necessary and sufficient for LAP to proceed. Subsequently, PS recruits the Rubicon-containing PI3-kinase complex to initiate the enzymatic cascade leading to LAP. Manipulation of plasma membrane PS content, PS binding by Rubicon or the PS-clustering domains of receptors prevents LAP and delays phagosome maturation. Therefore, the initiation of LAP represents a novel mechanism of PS-mediated signal transduction following ligation of surface receptors.

Indexed as

Microtubule-Associated ProteinsPhagocytosisPhosphatidylserinesReceptors, Cell SurfaceAdaptor Proteins, Signal TransducingAnimalsAutophagyAutophagy-Related ProteinsCell MembraneHumansIntracellular Signaling Peptides and ProteinsMacrophagesMicePhagosomesPhosphatidylinositol 3-KinasesSignal TransductionAdaptor Proteins, Signal TransducingAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsMAP1LC3A protein, humanMicrotubule-Associated ProteinsPhosphatidylinositol 3-KinasesPhosphatidylserinesReceptors, Cell SurfaceRUBCN protein, human

Identifiers

PMID40983659
PMCPMC12527911

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.