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Cited by 116Autophagy in Disease and TherapyPhagocytosis and Immune RegulationTuberculosis Research and Epidemiology

LC3-Associated Phagocytosis (LAP): Connections with Host Autophagy

Open access
Lai, Shu-chin, Devenish, Rodney J.·2012·Cells
DOI 10.3390/cells1030396PMC PMC3901117
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Abstract

Autophagy is an intracellular degradative process with a number of roles, one of which can be the protection of eukaryotic cells from invading microbes. Microtubule-associated protein light-chain 3 (LC3) is a key autophagy-related protein that is recruited to the double-membrane autophagosome responsible for sequestering material intended for delivery to lysosomes. GFP-LC3 is widely used as a marker of autophagosome formation as denoted by the formation of green puncta when viewed by fluorescence microscopy. Recently, it has been demonstrated that LC3 can be recruited to other membranes including single-membrane phagosomes, in a process termed LC3-associated phagocytosis (LAP). Thus, the observation of green puncta in cells can no longer, by itself, be taken as evidence of autophagy. This review will clarify those features of LAP which serve to distinguish it from autophagy and that make connections with host autophagic responses in terms of infection by microbial pathogens. More specifically, it will refer to concurrent studies of the mechanism by which LAP is triggered in comparison to autophagy.

AI snapshot

Written from the paper’s full text.

TL;DR

LC3-associated phagocytosis (LAP) recruits LC3 to single-membrane phagosomes, distinguishing it from canonical double-membrane autophagy. This review summarizes evidence that LAP contributes to pathogen degradation and dead-cell clearance, while noting that the trigger for LC3 recruitment and a reliable LAP-specific marker remain unresolved.

Key findings

  • LC3 can be recruited directly to single-membrane phagosomes, not only to double-membrane autophagosomes; therefore GFP-LC3 puncta alone cannot be taken as evidence of autophagy.
  • LAP occurs after phagocytosis of pathogens, apoptotic/necrotic cells, entotic cells, and micropinosomes; in RAW macrophage-like cells expressing GFP-LC3, LC3 translocated to phagosomes within 5 to 10 minutes of internalization of *E. coli* or yeast.
  • LAP requires the Atg5–Atg12–Atg16L conjugating system: knockout of *ATG5* or *ATG7* significantly reduced LC3 surrounding phagosomes containing bacteria, apoptotic bodies, or live cells.
  • ULK1 is not needed for LAP, whereas canonical autophagy involves at least 30 autophagy-related proteins and mammalian cells contain at least 8 LC3 homologues divided into two subfamilies.

Methods

  • Narrative review synthesizing published studies on autophagy and LC3-associated phagocytosis.
  • No primary experimental data, sample, or new statistical analysis are reported; evidence is drawn from cited cell-culture, infection, and electron-microscopy studies.
  • The paper organizes findings into figures and tables, including possible LAP triggers and published observations of single-membrane structures.

Limitations

  • The paper states that the exact mechanism(s) responsible for triggering LAP is still to be determined.
  • The paper states that there is no readily applicable technique to determine whether GFP-LC3 puncta co-localized with bacteria represent LAP or canonical autophagy; available methods require TEM ultrastructure or Atg-gene dependency tests.
  • The paper states that no exhaustive investigation of Atg protein requirements for LAP has been published and that a specific LAP marker or pharmacological reagent active against LAP is still needed; as a review, its conclusions depend on the cited literature.

Model-written summary. Check it against the paper before relying on it.

Integrity signals

Registry

Crossref · 10.3390/cells1030396

Cites

60 of 60 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

Claims the paper makes

29 of 43 cited sources checked · 13 supported · 0 flagged · accuracy not yet measured

  • Premisecitation

    LC3 can be recruited to single-membrane phagosomes in a process termed LC3-associated phagocytosis (LAP).

    “Recently, it has been demonstrated that LC3 can be recruited to other membranes including single-membrane phagosomes, in a process termed LC3-associated phagocytosis (LAP).”
    • Also stated in: § 1. Introduction · boosted
      “Recent research has shown that microtubule-associated protein light-chain (LC3), previously considered to be exclusively an autophagic marker, is also involved in LC3-associated phagocytosis (LAP) [12,13,14,15,16,17]”
    Quote in the paperSubstantial claim5 of 6 sources checked
    • cites [12] Florey, 2011, Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes, Nat. Cell Biol. source
    • cites [13] Gong, 2011, The Burkholderia pseudomallei Type III Secretion System and BopA Are Required for Evasion of LC3-Associated Phagocytosis, PLoS One source
    • cites [14] Huang, 2009, Activation of antibacterial autophagy by NADPH oxidases, Proc. Natl. Acad. Sci. USA source

      The section on FcγR- and TLR-induced recruitment reports LC3 on phagosomes, including phagosomes containing IgG-coated beads. Our copy does not specify that these phagosomes have a single membrane or call the process LC3-associated phagocytosis (LAP). (LLM, conf=0.82)

      Experimental — accuracy not yet measured
    • cites [15] Lerena, 2011, Mycobacterium marinum induces a marked LC3 recruitment to its containing phagosome that depends on a functional ESX-1 secretion system, Cell Microbiol. source

      The Discussion (page unavailable) states that most LC3-decorated M. marinum phagosomes had a single bilayer, supporting LC3 recruitment to single-membrane phagosomes. Our copy does not call this process LC3-associated phagocytosis (LAP); the GFP-LC3 results section also reports occasional fusion of an autophagosome with a phagosome, so the paper does not establish that its observed recruitment is specifically LAP. (LLM, conf=0.83)

      Experimental — accuracy not yet measured
    • cites [16] Martinez, 2011, Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells, Proc. Natl. Acad. Sci. USA source
    • cites [17] Sanjuan, 2008, Eating for good health: Linking autophagy and phagocytosis in host defense, Autophagy source

      The Intracellular Pathogens Surrender to Autophagy section says LC3 is conjugated directly to the phagosome without forming an autophagosome. Figure 1 contrasts this single-membrane process with double-membrane autophagy. Our copy does not call the process “LC3-associated phagocytosis” or “LAP.” (LLM, conf=0.83)

      Experimental — accuracy not yet measured
  • Premisecitation

    In Caenorhabditis elegans, LGG-1 (homolog of LC3) is recruited to the apoptotic Q neuroblast (Q cell) corpse.

    “Similarly, in Caenorhabditis elegans, LGG-1 (homolog of LC3) is recruited to the apoptotic Q neuroblast (Q cell) corpse [34].”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [34] Li, W., Zou, W., Yang, Y., Chai, Y., Chen, B., Cheng, S., Tian, D., Wang, X., Vale, R.D., and Ou, G. (2012). Autophagy genes function sequentially to promote apoptotic cell corpse degradation in the engulfing cell. J. Cell Biol. source
  • Premisecitation

    Infection of phagocytic neutrophils or non-phagocytic MEF cells expressing GFP-LC3 by Salmonella typhimurium resulted in recruitment of GFP-LC3 to bacteria-containing phagosomes.

    “Similarly, infection of either phagocytic neutrophils or non-phagocytic mouse embryonic fibroblast (MEF) cells, each expressing GFP-LC3, by Salmonella typhimurium also resulted in the recruitment of GFP-LC3 to bacteria-containing phagosomes [14,33].”
    Quote in the paperSubstantial claim2 of 2 sources checked
    • cites [14] Huang, 2009, Activation of antibacterial autophagy by NADPH oxidases, Proc. Natl. Acad. Sci. USA source

      The NOX2-Generated ROS section (page unavailable) reports that GFP-LC3-expressing neutrophils infected with S. Typhimurium had LC3 colocalized with bacteria in LAMP1-positive phagosomes. The Materials and Methods section (page unavailable) lists the cell lines used, but our copy does not report the claimed Salmonella experiment in mouse embryonic fibroblasts. (LLM, conf=0.89)

      Experimental — accuracy not yet measured
    • cites [33] Kageyama, 2011, The LC3 recruitment mechanism is separate from Atg9L1-dependent membrane formation in the autophagic response against Salmonella, Mol. Biol. Cell source

      The Results section, “LC3 associates with S. typhimurium through an LC3-lipidation reaction” (page unavailable), reports that GFP-LC3 surrounded S. typhimurium in infected MEFs. Our copy does not establish the corresponding finding in neutrophils or identify the LC3-positive structures as bacteria-containing phagosomes. (LLM, conf=0.87)

      Experimental — accuracy not yet measured
  • Premisecitation

    Invading pathogens are recognized by mammalian cells through receptors found either at the cell surface (e.g., TLRs) or in the cytoplasm (NLRs).

    “Invading pathogens are recognized by mammalian cells through receptors found either at the cell surface (eg, trans-membrane Toll-like Receptors; TLRs), or in the cytoplasm (Nod-like Receptors (NLRs) [36,37].”
    Quote in the paperNot a substantial claim2 of 2 sources checked
    • cites [36] Freche, 2007, The role of the inflammasome in cellular responses to toxins and bacterial effectors, Semin. Immunopathol. source
    • cites [37] Xu, 2007, Toll-like receptor 4 is a sensor for autophagy associated with innate immunity, Immunity source

      The Introduction states that TLRs detect microbes, and the Results show that TLR4 mediates a response to bacterial LPS. Our copy does not establish the claimed cell-surface location of TLRs or discuss cytoplasmic NLRs, so it supports only the TLR recognition part of the sentence. (LLM, conf=0.86)

      Experimental — accuracy not yet measured
  • Premisecitation

    LC3 decorated Mycobacterium marinum-containing phagosomes after infection of RAW cells.

    “Furthermore, by following the indirect immunofluorescence staining of endogenous LC3, Lerena and Colombo [15] showed that LC3 decorated Mycobacterium marinum-containing phagosomes after infection of RAW cells.”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [15] Lerena, 2011, Mycobacterium marinum induces a marked LC3 recruitment to its containing phagosome that depends on a functional ESX-1 secretion system, Cell Microbiol. source
  • Classified as probably not a substantial claim. 11
  • May combine two claims. 12

  • Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

    Premisecitation

    LC3 can associate with other cellular components including microtubules and the osteoclast ruffled border observed in bone resorption.

    “LC3 can also associate with other cellular components including microtubules [19] and the osteoclast ruffled border observed in bone resorption [20].”
    Quote in the paperNot a substantial claim2 of 2 sources checked
    • cites [19] Khalil, 2011, Autophagy-independent function of MAP-LC3 during intracellular propagation of Chlamydia trachomatis, Autophagy source
    • cites [20] DeSelm, 2011, Autophagy proteins regulate the secretory component of osteoclastic bone resorption, Dev. Cell source

  • Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

    Premisecitation

    Prior to fusion of autophagosomes with lysosomes, LC3-II on the outer autophagosomal membrane is released by deconjugation of PE from LC3 by Atg4, while LC3-II associated with the inner membrane is retained and eventually degraded by acid hydrolases within the autophagolysosome.

    “Prior to the fusion of autophagosomes with lysosomes, the LC3-II located on the outer autophagosomal membrane is released by deconjugation of PE from LC3 by the proteolytic activity of Atg4. By contrast, LC3-II associated with the inner membrane is retained, although eventually degraded by the acid hydrolases within the autophagolysosome [27].”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [27] Noda, 2008, The Ubi brothers reunited, Autophagy source

      Split into 2 atoms — 0 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 1 unverifiable. Expand the claim to see per-atom verdicts.

      Experimental — accuracy not yet measured

  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    LC3B is widely used as a fusion with GFP (GFP-LC3) to follow autophagosome formation using fluorescence microscopy.

    “LC3B is the protein that is widely used as a fusion with GFP (GFP-LC3) to follow autophagosome formation using fluorescence microscopy [31].”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [31] Klionsky, 2008, Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes, Autophagy source

  • May combine two claims.

    Premisecitation

    Recent work indicates the two LC3 subfamilies act differently at early stages of autophagosome biogenesis: the LC3 subfamily is required for elongation of the phagophore membrane, whereas the GABARAP/GATE subfamily is required for a later stage in autophagosome maturation.

    “Recent work has indicated that the two subfamilies act differently at early stages of autophagosome biogenesis. Thus, the LC3 subfamily is required for elongation of the phagophore membrane, whereas the GABARAP/GATE subfamily is required for a later stage in autophagosome maturation [32]”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [32] Weidberg, 2010, LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis, EMBO J. source

  • Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

    Premisecitation

    Cytosolic LC3-I is conjugated to phosphatidylethanolamine (PE), and in this form LC3-II is recruited to the growing autophagosome membrane.

    “The cytosolic form of LC3 (designated LC3-I) is conjugated to phosphatidylethanolamine (PE) and in this form (designated LC3-II) it is recruited to the growing autophagosome membrane [26].”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [26] Kabeya, 2000, LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing, EMBO J. source

      The sections on LC3 processing and autophagosome-membrane localization report conversion of cytosolic LC3-I to LC3-II and association of LC3-II with autophagosome membranes (page numbers unavailable). Our copy does not identify phosphatidylethanolamine as the conjugated molecule or establish recruitment specifically to a growing membrane. (LLM, conf=0.88)

      Experimental — accuracy not yet measured

  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    Two ubiquitin-like conjugation systems contribute to autophagosome formation.

    “Two ubiquitin-like conjugation systems also contribute to autophagosome formation [23,24,25].”
    Quote in the paperNot a substantial claim1 of 3 sources checked
    • cites [23] Yang, 2010, Mammalian autophagy: Core molecular machinery and signaling regulation, Curr. Opin. Cell Biol. source
    • cites [24] Itakura, 2010, Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins, Autophagy source
    • cites [25] Hanada, 2007, The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy, J. Biol. Chem. source

  • May combine two claims.

    Premisecitation

    In LAP, LC3 is recruited directly to the single-membrane phagosome, distinct from conventional autophagy where LC3 is incorporated into the double-membrane autophagosome.

    “In LAP, distinct from the conventional autophagic pathway where LC3 is incorporated into the double-membrane autophagosome, LC3 is recruited directly to the single-membrane phagosome [12,16,18].”
    Quote in the paperSubstantial claim1 of 3 sources checked
    • cites [12] Florey, 2011, Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes, Nat. Cell Biol. source
    • cites [16] Martinez, 2011, Microtubule-associated protein 1 light chain 3 alpha (LC3)-associated phagocytosis is required for the efficient clearance of dead cells, Proc. Natl. Acad. Sci. USA source
    • cites [18] Sanjuan, 2007, Toll-like receptor signalling in macrophages links the autophagy pathway to phagocytosis, Nature source

  • May combine two claims.

    Premisecitation

    In Burkholderia pseudomallei infection of GFP-LC3 expressing RAW macrophage cells, intracellular bacteria reside within LC3-positive phagosomes, from which they later escape into the cytosol.

    “In the case of Burkholderia pseudomallei infection of GFP-LC3 expressing RAW macrophage cells, the intracellular bacteria reside within LC3-positive phagosomes [13], from which they later escape into the cytosol.”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [13] Gong, 2011, The Burkholderia pseudomallei Type III Secretion System and BopA Are Required for Evasion of LC3-Associated Phagocytosis, PLoS One source

      The Results section (page unavailable) reports that approximately 5–10% of wild-type bacteria were associated with LC3 at 2 hours and suggests that LC3 is recruited to bacteria-containing phagosomes. Figure 2 says that most wild-type bacteria escape from phagosomes into the cytosol, but the paper does not show that they escape specifically from LC3-positive phagosomes. The claim also omits that LC3 association was observed in only a small subset. (LLM, conf=0.86)

      Experimental — accuracy not yet measured

  • May combine two claims.

    Premisecitation

    The internalised cell in a phagosome is decorated by LC3 and itself undergoes programmed cell death.

    “The internalised cell in a phagosome is shown to be decorated by LC3 and itself undergoes programmed cell death [12].”
    Quote in the paperNot a substantial claim1 of 1 sources checked
    • cites [12] Florey, 2011, Autophagy machinery mediates macroendocytic processing and entotic cell death by targeting single membranes, Nat. Cell Biol. source

      The Introduction says LC3 is recruited to the entotic vacuole membrane surrounding an internalized cell, and that the cell is subsequently killed by its host. The Results section on apoptotic cell phagosomes likewise places LC3 on the phagosome membrane, not on the internalized cell itself. Thus the claim captures LC3 recruitment and cell death but misidentifies what LC3 decorates. (LLM, conf=0.87)

      Experimental — accuracy not yet measured

  • May combine two claims.

    Interpretationreasoning

    LAP has a number of different roles in the cell that include maintenance of cellular homeostasis and protection against invading pathogens.

    “Hence, LAP has a number of different roles in the cell that include maintenance of cellular homeostasis and protection against invading pathogens.”
    Quote in the paperNot a substantial claim

  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    The second GABARAP/GATE subfamily comprises GABARAP, GABARAPL1, GATE-16 (aka GABARAPL2) and GABARAP-L3.

    “The second, the GABARAP/GATE subfamily, comprises GABARAP, GABARAPL1, GATE-16 (aka GABARAPL2) and GABARAP-L3 [29,30].”
    Quote in the paperNot a substantial claim0 of 2 sources checked
    • cites [29] Xin, 2001, Cloning, expression patterns, and chromosome localization of three human and two mouse homologues of GABA(A) receptor-associated protein, Genomics source
    • cites [30] Kabeya, 2004, LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation, J. Cell Sci. source

  • Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

    Premisenone given

    One ubiquitin-like conjugation system requires LC3 and is considered essential for autophagy.

    “One of these systems requires the ubiquitin-like protein LC3 and is considered essential for autophagy.”
    Quote in the paperNot a substantial claim

  • May combine two claims.

    Premisecitation

    Both TLR- or FcγR-dependent NOX2 activity triggered formation of LC3-associated phagosomes that eventually fused with lysosomes and the invading pathogens were degraded.

    “Both TLR- or FcγR-dependent NOX2 activity triggered the formation of LC3-associated phagosomes that eventually fused with lysosomes and the invading pathogens were degraded.”
    Quote in the paperSubstantial claim

  • Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

    Premisenone given

    Mammalian cells contain at least 8 LC3 homologues divided into two subfamilies based on amino acid sequence.

    “Interestingly, mammalian cells contain at least 8 LC3 homologues divided into two subfamilies based on amino acid sequence.”
    Quote in the paperNot a substantial claim

  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    Entosis is a live-cell engulfment pathway occurring between two neighbouring cells, one of which will be actively engulfed by the other to form a cell-in-cell structure.

    “Entosis is a live-cell engulfment pathway occurring between two neighbouring cells, one of which will be actively engulfed by the other to form a ‘cell-in-cell’ structure [35].”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites [35] Overholtzer, 2007, A nonapoptotic cell death process, entosis, that occurs by cell-in-cell invasion, Cell source

  • Probably not a substantial claim: may not pass S3 (load-bearing).

    Premisecitation

    The first LC3 subfamily comprises LC3A (including 2 splicing variants), LC3B and LC3C.

    “The first LC3 subfamily comprises LC3A (including 2 splicing variants), LC3B and LC3C [28].”
    Quote in the paperNot a substantial claim0 of 1 sources checked
    • cites [28] He, 2003, Post-translational modifications of three members of the human MAP1LC3 family and detection of a novel type of modification for MAP1LC3B, J. Biol. Chem. source

  • Probably not a substantial claim: may not pass S3 (load-bearing). May combine two claims.

    Premisecitation

    Formation of the phagophore requires the ULK-Atg13-FIP200 complex, while its elongation requires the class III PI3K complex consisting of Vps34, Beclin 1 and Vps15.

    “The formation of the phagophore requires the activity of the ULK-Atg13-FIP200 complex, while its elongation requires the class III phosphatidylinositol 3-kinase (PI3K) complex consisting of Vps34, Beclin 1 and Vps15.”
    Quote in the paperNot a substantial claim
17 of 17

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Cited works that were retracted

Works this paper cites that were later retracted, from the retraction notices publishers deposit. Major when the notice came out before this paper was published.

  • Cites a retracted work: 10.1073/pnas.1113421108

    Info

    The cited work was retracted on 2025-08-04 (notice 10.1073/pnas.2518460122), not before this paper was published (2012-07-30).

    Cited work 10.1073/pnas.1113421108 · retracted 2025-08-04 · notice 10.1073/pnas.2518460122 · this paper published 2012-07-30

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Related

Authors
Lai, S.-C., & Devenish, R. J.
Affiliations
Monash University (AU)
Corresponding author
Devenish, Rodney J.
ORCID
Venue
Cells
Publisher
MDPI AG
Published
2012-07-30
Volume
1
Issue
3
Pages
396-408
ISSN
2073-4409 (ISSN-L)
DOI
10.3390/cells1030396
PMC
PMC3901117
OpenAlex
W2067656942
Semantic Scholar
60df618c7e2b97011b8cc1e1bbcd05c5d1899333
Cited by
116
References
60
Citations by year
2026: 4 · 2025: 7 · 2024: 3 · 2023: 6 · 2022: 9 · 2021: 9 · 2020: 14 · 2019: 10 · 2018: 8 · 2017: 10 · 2016: 16 · 2015: 7 · 2014: 11 · 2013: 2
FWCI
4.33
Type
journal article
Language
en
Open access
Licence
Locations
  • Cells (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (submittedVersion, cc-by)
  • PubMed Central (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Medical Research Council
  • Australian Research Council
  • National Health and Medical Research Council
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
  • Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
Keywords
LC3-associated phagocytosis, autophagy, LC3, autophagosome formation, phagosome, GFP-LC3, phagocytosis

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