id: Q09490
gene_symbol: lgg-1
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
description: 'LGG-1 is the C. elegans GABARAP/ATG8 family ortholog and a central ubiquitin-like
  modifier in macroautophagy. The protein is proteolytically cleaved at Gly-116 by
  ATG-4.1/ATG-4.2, then conjugated to phosphatidylethanolamine (PE) via the ATG7-ATG3-ATG12/5/16
  conjugation system, anchoring it to autophagosomal membranes. LGG-1 functions primarily
  in autophagosome biogenesis and acts upstream of LGG-2 (the LC3-like paralog), recruiting
  LGG-2 to maturing autophagosomes. LGG-1 directly binds LIR motif-containing cargo
  receptors including SEPA-1 (for P granule degradation), SQST-1/p62, ALLO-1 (for
  paternal mitochondrial elimination), and the autophagy machinery components UNC-51,
  ATG-13, and EPG-7. GFP::LGG-1 puncta are the gold-standard autophagy reporter in
  C. elegans. LGG-1 is essential for dauer development, longevity, selective autophagy
  pathways (aggrephagy, mitophagy, xenophagy, allophagy), and stress resistance. Recent
  work (2023) shows that while C-terminal cleavage is essential for autophagosome
  initiation, PE lipidation is not strictly required for autophagy and development
  but enhances cargo recognition efficiency and LGG-2 autophagosome formation.

  '
existing_annotations:
- term:
    id: GO:0000045
    label: autophagosome assembly
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'LGG-1 is a core component of the autophagosome assembly machinery. As
      an ATG8 family protein, it is conjugated to PE on the isolation membrane/phagophore
      and drives membrane expansion. This annotation is well-supported by phylogenetic
      inference from characterized orthologs (Atg8, LC3, GABARAP).

      '
    action: ACCEPT
    reason: 'LGG-1 is essential for autophagosome assembly in C. elegans. Multiple
      studies demonstrate that LGG-1 localizes to autophagosomes and is required for
      their formation (PMID:12958363, PMID:24374177, PMID:37395461). UniProt describes
      LGG-1 as a "Ubiquitin-like modifier involved in the formation of autophagosomal
      vacuoles (autophagosomes)". The 2023 eLife paper (PMID:37395461) confirms that
      C-terminal cleavage of LGG-1 is essential for autophagosome initiation and biogenesis.
      The deep research (file:worm/lgg-1/lgg-1-deep-research-falcon.md) confirms "LGG-1
      is the Caenorhabditis elegans ortholog of the ATG8/LC3/GABARAP family".

      '
    supported_by:
    - reference_id: PMID:37395461
      supporting_text: the cleavage of the C-terminus from the precursor is 
        essential for the functionality of LGG-1(G116A)
    - reference_id: PMID:12958363
      supporting_text: Dauer formation is associated with increased autophagy 
        and also requires C. elegans orthologs of the yeast autophagy genes 
        APG1, APG7, APG8, and AUT10.
- term:
    id: GO:0000421
    label: autophagosome membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'LGG-1 localizes to autophagosome membranes through its lipidation with
      PE at Gly-116. This localization is conserved across ATG8 family proteins.

      '
    action: ACCEPT
    reason: 'LGG-1 is conjugated to PE and anchors to autophagosome membranes, as
      demonstrated by fluorescent reporter studies and biochemical analyses (PMID:24374177,
      PMID:37395461). UniProt confirms subcellular location at "Cytoplasmic vesicle,
      autophagosome membrane."

      '
    supported_by:
    - reference_id: PMID:24374177
      supporting_text: The formation of the autophagic vesicles requires the 
        recruitment of ubiquitin-like Atg8 proteins to the membrane of nascent 
        autophagosomes.
    - reference_id: PMID:37395461
      supporting_text: the lipidation of LGG-1 appears to be important for the 
        coordination between cargo recognition and autophagosome biogenesis
- term:
    id: GO:0000423
    label: mitophagy
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'LGG-1 is directly involved in mitophagy in C. elegans, both in general
      mitochondrial quality control during aging and in the specialized allophagy
      pathway for paternal mitochondrial elimination after fertilization.

      '
    action: ACCEPT
    reason: 'Multiple studies demonstrate LGG-1 involvement in mitophagy. Palikaras
      et al. (PMID:25896323) showed LGG-1 localizes to mitochondria and is required
      for mitophagy during aging. Wang et al. (2016) demonstrated LGG-1-positive autophagosomes
      enclose paternal mitochondria during paternal mitochondrial elimination. The
      deep research (file:worm/lgg-1/lgg-1-deep-research-falcon.md) confirms "paternal
      mitochondria are selectively recognized and engulfed by LGG-1-positive autophagosomes"
      and describes "selective mitophagy during paternal mitochondrial elimination".

      '
    supported_by:
    - reference_id: PMID:25896323
      supporting_text: We find that DCT-1 is a key mediator of mitophagy and 
        longevity assurance under conditions of stress in C. elegans. Impairment
        of mitophagy compromises stress resistance
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: paternal mitochondria are selectively recognized and 
        engulfed by LGG-1-positive autophagosomes
- term:
    id: GO:0008429
    label: phosphatidylethanolamine binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'LGG-1 is covalently conjugated to PE at Gly-116, which is the biochemical
      basis for its membrane association during autophagy.

      '
    action: ACCEPT
    reason: 'LGG-1 is lipidated with PE through the ATG8 conjugation cascade. This
      is a well-characterized biochemical property of ATG8 family proteins. UniProt
      confirms the "Phosphatidylethanolamine amidated glycine" modification at position
      116. The PE conjugation is the direct molecular mechanism of membrane anchoring.

      '
    supported_by:
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: ATG8/LC3/GABARAP family of ubiquitin-like proteins that 
        are covalently conjugated to the autophagosomal membrane lipid 
        phosphatidylethanolamine (PE) during macroautophagy
- term:
    id: GO:0097352
    label: autophagosome maturation
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'LGG-1 functions in autophagosome maturation, acting upstream of LGG-2
      and recruiting it to maturing autophagosomes.

      '
    action: ACCEPT
    reason: 'Manil-Segalen et al. (PMID:24374177) demonstrated that LGG-1 acts upstream
      of LGG-2 in autophagosome maturation, with LGG-1 being required for LGG-2 recruitment
      to autophagosomes. LGG-2 then controls autophagosome-lysosome fusion. This establishes
      a clear role for LGG-1 in the maturation pathway.

      '
    supported_by:
    - reference_id: PMID:24374177
      supporting_text: During allophagy, a developmentally stereotyped 
        autophagic flux, LGG-1 acts upstream of LGG-2 to allow its localization 
        to autophagosomes. LGG-2 controls the maturation of LGG-1-positive 
        autophagosomes and facilitates the tethering with the lysosomes
- term:
    id: GO:0031625
    label: ubiquitin protein ligase binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'This annotation refers to binding of ATG8-family proteins to E1/E2-like
      enzymes in the conjugation pathway (ATG7, ATG3).

      '
    action: ACCEPT
    reason: 'LGG-1 directly interacts with ATG-7 (E1-like) and ATG-3 (E2-like) as
      part of the conjugation cascade that lipidates LGG-1 to PE. These interactions
      are direct and essential for LGG-1 function. The term "ubiquitin protein ligase
      binding" captures interaction with the ubiquitin-like modification machinery
      appropriately.

      '
    supported_by:
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: ATG7 (E1-like) activates ATG8; ATG3 (E2-like) transfers 
        it to PE on isolation membranes, with the ATG12-ATG5-ATG16 complex 
        facilitating lipidation
- term:
    id: GO:0050811
    label: GABA receptor binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'This annotation derives from the GABARAP name (GABA receptor-associated
      protein) of mammalian orthologs, but LGG-1''s role in GABA receptor binding
      in C. elegans is not experimentally validated. The GABARAP naming reflects a
      historical discovery context for mammalian proteins that does not apply to the
      C. elegans ortholog, which has no documented GABA receptor interactions.

      '
    action: REMOVE
    reason: 'This annotation has no supporting evidence in C. elegans. The GABA receptor
      binding function is a historical artifact of the mammalian GABARAP nomenclature
      and has not been demonstrated for LGG-1 in worms. LGG-1''s primary and extensively
      documented function is in autophagy machinery as an ATG8 family member. There
      is no experimental evidence in C. elegans literature demonstrating binding to
      GABA receptors or involvement in GABA receptor trafficking. This annotation
      should be removed entirely as it misrepresents the function of LGG-1.

      '
- term:
    id: GO:0006995
    label: cellular response to nitrogen starvation
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: 'Autophagy is induced by nutrient starvation including nitrogen starvation,
      and ATG8 family proteins are upregulated under these conditions.

      '
    action: ACCEPT
    reason: 'Autophagy is a conserved starvation response, and ATG8/LGG-1 is essential
      for this process. While direct evidence for nitrogen starvation specifically
      is limited in C. elegans, the dauer pathway (induced by starvation conditions)
      requires LGG-1 (PMID:12958363). The annotation is phylogenetically sound.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: Autophagy, through the sequestration and delivery of 
        cargo to the lysosomes, is the major route for degrading long-lived 
        proteins and cytoplasmic organelles in eukaryotic cells.
- term:
    id: GO:0000407
    label: phagophore assembly site
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 localizes to the phagophore assembly site/preautophagosomal structure
      where autophagosomes are nucleated.

      '
    action: ACCEPT
    reason: 'UniProt confirms subcellular location at "Preautophagosomal structure"
      based on experimental evidence (PMID:12958363, PMID:17327275). This is consistent
      with LGG-1''s role in autophagosome biogenesis.

      '
    supported_by:
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: ATG8 dosage controls phagophore expansion and 
        autophagosome size; the LGG-1 paralog executes analogous functions in 
        worms to promote autophagosome membrane growth and maturation
- term:
    id: GO:0000421
    label: autophagosome membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'Duplicate of the IBA annotation. LGG-1 localizes to autophagosome membranes.

      '
    action: ACCEPT
    reason: 'This is consistent with the IBA annotation and experimentally validated.
      Multiple IDA annotations confirm autophagosome membrane localization.

      '
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 is found in the cytoplasm in its unlipidated, soluble form.

      '
    action: ACCEPT
    reason: 'LGG-1 cycles between cytosolic (unlipidated) and membrane-bound (lipidated)
      forms. UniProt confirms cytoplasmic localization with multiple IDA evidence.

      '
    supported_by:
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: LGG-1 cycles between diffuse cytosolic and punctate 
        membrane-associated forms
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 localizes to mitochondria during mitophagy processes.

      '
    action: ACCEPT
    reason: 'UniProt confirms mitochondrial localization (PMID:25896323). LGG-1 autophagosomes
      enclose mitochondria during mitophagy and allophagy. The IDA annotation for
      mitochondrial outer membrane (PMID:25896323) supports this.

      '
    supported_by:
    - reference_id: PMID:25896323
      supporting_text: We find that DCT-1 is a key mediator of mitophagy and 
        longevity assurance under conditions of stress in C. elegans
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 is a definitive marker of autophagosomes.

      '
    action: ACCEPT
    reason: 'GFP::LGG-1 puncta are the gold-standard autophagosome marker in C. elegans.
      Multiple IDA annotations confirm this localization (PMID:12958363, PMID:22560223,
      PMID:24882217). The deep research confirms "GFP::LGG-1 puncta mark forming autophagosomes."

      '
    supported_by:
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: GFP::LGG-1 puncta mark forming autophagosomes
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 can localize to the plasma membrane, particularly the cell membrane.

      '
    action: ACCEPT
    reason: 'UniProt indicates cell membrane localization with lipid-anchor evidence
      (PMID:24185444, PMID:26687600). This may relate to non-canonical autophagy functions
      or membrane repair processes.

      '
- term:
    id: GO:0006914
    label: autophagy
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: 'LGG-1 is a core autophagy protein.

      '
    action: ACCEPT
    reason: 'This is the parent term and is fully supported by extensive experimental
      evidence. LGG-1 is essential for autophagy in C. elegans.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: autophagy genes are essential for dauer development and 
        life-span extension in C. elegans
- term:
    id: GO:0030425
    label: dendrite
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 localizes to dendrites in neurons.

      '
    action: ACCEPT
    reason: 'UniProt confirms dendritic localization based on experimental evidence
      from neuronal studies. Hill et al. (PMID:30880001) showed LGG-1 in neuronal
      compartments including neuron projections.

      '
- term:
    id: GO:0030670
    label: phagocytic vesicle membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 localizes to phagosome membranes during LC3-associated phagocytosis-like
      processes.

      '
    action: ACCEPT
    reason: 'UniProt confirms phagosome membrane localization (PMID:22451698). LGG-1
      is involved in apoptotic cell clearance and localizes to phagosomes during engulfment
      processes. This is relevant to LAP-like functions. The deep research confirms
      "LGG-1 and LGG-2 puncta transiently localize adjacent to phagosomes."

      '
    supported_by:
    - reference_id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
      supporting_text: LGG-1 and LGG-2 puncta transiently localize adjacent to 
        phagosomes; marker entry indicates autophagosome-phagosome fusion events
- term:
    id: GO:0031410
    label: cytoplasmic vesicle
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: 'LGG-1 localizes to cytoplasmic vesicles (autophagosomes).

      '
    action: ACCEPT
    reason: 'Autophagosomes are cytoplasmic vesicles. This is a parent term that is
      appropriately general.

      '
- term:
    id: GO:0043202
    label: lysosomal lumen
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 is delivered to the lysosomal lumen as part of autophagosome-lysosome
      fusion.

      '
    action: ACCEPT
    reason: 'UniProt confirms lysosome lumen localization (PMID:24374177). LGG-1 on
      the inner autophagosomal membrane is delivered to the lysosomal lumen where
      it is degraded along with cargo.

      '
    supported_by:
    - reference_id: PMID:24374177
      supporting_text: LGG-2 controls the maturation of LGG-1-positive 
        autophagosomes and facilitates the tethering with the lysosomes
- term:
    id: GO:0043204
    label: perikaryon
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: 'LGG-1 localizes to the neuronal cell body (perikaryon).

      '
    action: ACCEPT
    reason: 'UniProt confirms perikaryon localization based on neuronal studies (PMID:30880001).
      This is consistent with the IDA annotation for neuronal cell body.

      '
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:14704431
  review:
    summary: 'LGG-1 interacts with ATG-4.1 based on C. elegans interactome mapping.

      '
    action: MODIFY
    reason: 'The term "protein binding" is uninformative. LGG-1 specifically interacts
      with ATG-4.1, which is its processing protease. A more specific term like "cysteine-type
      endopeptidase binding" or retaining as-is with the understanding that the WITH/FROM
      column specifies ATG-4.1 is acceptable, but the annotation should ideally be
      more specific. The interaction is functionally relevant as ATG-4.1 cleaves LGG-1
      to expose Gly-116.

      '
    proposed_replacement_terms:
    - id: GO:0044877
      label: protein-containing complex binding
    supported_by:
    - reference_id: PMID:14704431
      supporting_text: Jan 2. A map of the interactome network of the metazoan 
        C.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19123269
  review:
    summary: 'LGG-1 interacts with ATG-4.1 based on controlled interactome mapping.

      '
    action: MODIFY
    reason: 'Same as above - protein binding is too general. The interaction with
      ATG-4.1 is the proteolytic enzyme that processes LGG-1.

      '
    proposed_replacement_terms:
    - id: GO:0044877
      label: protein-containing complex binding
    supported_by:
    - reference_id: PMID:19123269
      supporting_text: Empirically controlled mapping of the Caenorhabditis 
        elegans protein-protein interactome network.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19167332
  review:
    summary: 'LGG-1 directly interacts with SEPA-1, the P granule autophagy receptor.

      '
    action: MODIFY
    reason: 'This is a functionally important interaction - SEPA-1 is a cargo receptor
      that bridges P granule components to LGG-1 for selective degradation. The paper
      demonstrates direct binding via LIR motifs. A more specific MF term capturing
      LIR-dependent interaction would be preferable.

      '
    proposed_replacement_terms:
    - id: GO:0044877
      label: protein-containing complex binding
    additional_reference_ids:
    - PMID:26687600
    supported_by:
    - reference_id: PMID:19167332
      supporting_text: SEPA-1 directly binds to the P granule component PGL-3 
        and also to the autophagy protein LGG-1/Atg8. SEPA-1 aggregates 
        consistently colocalize with PGL granules and with LGG-1 puncta.
    - reference_id: PMID:26687600
      supporting_text: Structural Basis of the Differential Function of the Two 
        C.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23619095
  review:
    summary: 'LGG-1 interacts with AIN-1, a component of the miRNA-induced silencing
      complex.

      '
    action: ACCEPT
    reason: 'This interaction is related to autophagy-mediated regulation of miRNA
      silencing. AIN-1/GW182 is an autophagy substrate. While "protein binding" is
      generic, this is an interesting regulatory interaction. The IntAct database
      confirms LGG-1-AIN-1 interaction.

      '
    supported_by:
    - reference_id: PMID:23619095
      supporting_text: Autophagy modulates miRNA-mediated gene silencing and 
        selectively degrades AIN-1/GW182 in C.
- term:
    id: GO:0070266
    label: necroptotic process
  evidence_type: IGI
  original_reference_id: PMID:22157748
  review:
    summary: 'LGG-1 contributes to necrotic neurodegeneration in ion channel mutants.

      '
    action: KEEP_AS_NON_CORE
    reason: 'This is not a core function of LGG-1 but rather represents a context
      where autophagy genes contribute to cell death. Troulinaki and Tavernarakis
      (PMID:22157748) showed that endocytosis synergizes with autophagy in necrotic
      neurodegeneration. Earlier work (PMID:17327275) showed that lgg-1 inactivation
      partially suppresses ion-channel-dependent neuronal degeneration. This is a
      pleiotropic consequence of autophagy function rather than a core role.

      '
    supported_by:
    - reference_id: PMID:17327275
      supporting_text: Inactivation of unc-51, bec-1 and lgg-1, the worm 
        counterparts of the yeast autophagy genes Atg1, Atg6 and Atg8 
        respectively, partially suppresses degeneration of neurons with toxic 
        ion channel variants.
    - reference_id: PMID:22157748
      supporting_text: Endocytosis and intracellular trafficking contribute to 
        necrotic neurodegeneration in C.
- term:
    id: GO:0008340
    label: determination of adult lifespan
  evidence_type: IMP
  original_reference_id: PMID:28198373
  review:
    summary: 'LGG-1 is required for lifespan extension by hormetic heat stress.

      '
    action: KEEP_AS_NON_CORE
    reason: 'While LGG-1 is required for lifespan extension in multiple longevity
      paradigms, this is a downstream consequence of its core autophagy function rather
      than a primary function. Kumsta et al. (PMID:28198373) showed that lgg-1 RNAi
      reduces the extended lifespan of animals exposed to hormetic heat shock. This
      represents a pleiotropic effect of autophagy on aging.

      '
    supported_by:
    - reference_id: PMID:28198373
      supporting_text: Here, too, we found that autophagy genes (unc-51/ATG1, 
        bec-1/ATG6, lgg-1/ATG8, atg-18 and atg-13; the latter two involved in 
        phagophore formation) were required for the increased lifespan of 
        wild-type animals exposed to hormetic heat shock early in life
- term:
    id: GO:0009408
    label: response to heat
  evidence_type: IMP
  original_reference_id: PMID:28198373
  review:
    summary: 'LGG-1 is induced by heat stress and required for heat stress resistance.

      '
    action: KEEP_AS_NON_CORE
    reason: 'Autophagy induction by heat stress is well-documented, and LGG-1 is required
      for the beneficial effects of hormetic heat stress. However, this is a stress-responsive
      function rather than a core molecular function.

      '
    supported_by:
    - reference_id: PMID:28198373
      supporting_text: heat shock increased autophagosome numbers with different
        kinetics in each of the examined tissues
- term:
    id: GO:0016236
    label: macroautophagy
  evidence_type: IMP
  original_reference_id: PMID:28198373
  review:
    summary: 'LGG-1 is essential for macroautophagy.

      '
    action: ACCEPT
    reason: 'This is the core function of LGG-1. As an ATG8 family protein, LGG-1
      is essential for the macroautophagy pathway. Multiple studies confirm this role.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: Autophagy, through the sequestration and delivery of 
        cargo to the lysosomes, is the major route for degrading long-lived 
        proteins and cytoplasmic organelles in eukaryotic cells.
    - reference_id: PMID:28198373
      supporting_text: Hormetic heat stress and HSF-1 induce autophagy to 
        improve survival and proteostasis in C.
- term:
    id: GO:0001778
    label: plasma membrane repair
  evidence_type: IMP
  original_reference_id: PMID:27875098
  review:
    summary: 'LGG-1 contributes to plasma membrane repair after pore-forming toxin
      damage.

      '
    action: KEEP_AS_NON_CORE
    reason: 'Chen et al. (PMID:27875098) demonstrated that autophagy contributes to
      membrane pore repair in response to bacterial toxins. This is an interesting
      specialized function but represents an application of the core autophagy machinery
      rather than a primary function of LGG-1.

      '
    supported_by:
    - reference_id: PMID:27875098
      supporting_text: autophagy controls the susceptibility of animals to PFT 
        toxicity through xenophagic degradation of PFT and repair of 
        membrane-pore cell-autonomously in the PFT-targeted intestinal cells in 
        C. elegans
- term:
    id: GO:0097237
    label: cellular response to toxic substance
  evidence_type: IMP
  original_reference_id: PMID:27875098
  review:
    summary: 'LGG-1 is involved in defense against bacterial pore-forming toxins.

      '
    action: KEEP_AS_NON_CORE
    reason: 'Autophagy-mediated defense against toxins is a protective response utilizing
      the core autophagy machinery. Chen et al. showed LGG-1 is induced by and required
      for defense against Cry5B toxin.

      '
    supported_by:
    - reference_id: PMID:27875098
      supporting_text: bacterial membrane pore-forming toxin (PFT) induces 
        autophagy in an HLH-30-dependent manner in Caenorhabditis elegans
- term:
    id: GO:0098792
    label: xenophagy
  evidence_type: IMP
  original_reference_id: PMID:27875098
  review:
    summary: 'LGG-1 is required for xenophagic degradation of bacterial toxins.

      '
    action: ACCEPT
    reason: 'Xenophagy is a selective autophagy pathway that uses the core autophagy
      machinery including LGG-1. Chen et al. demonstrated xenophagic degradation of
      Cry5B toxin requires LGG-1. This is a bona fide selective autophagy function
      for LGG-1.

      '
    supported_by:
    - reference_id: PMID:27875098
      supporting_text: autophagy controls the susceptibility of animals to PFT 
        toxicity through xenophagic degradation of PFT and repair of 
        membrane-pore cell-autonomously in the PFT-targeted intestinal cells in 
        C. elegans
- term:
    id: GO:0043005
    label: neuron projection
  evidence_type: IDA
  original_reference_id: PMID:30880001
  review:
    summary: 'LGG-1 localizes to neuron projections in AIY interneurons.

      '
    action: ACCEPT
    reason: 'Hill et al. (PMID:30880001) used fluorescent reporters to demonstrate
      LGG-1 localization in neuronal compartments including projections. UniProt confirms
      neuron projection localization.

      '
    supported_by:
    - reference_id: PMID:30880001
      supporting_text: Epub 2019 Mar 14. Maturation and Clearance of 
        Autophagosomes in Neurons Depends on a Specific Cysteine Protease 
        Isoform, ATG-4.2.
- term:
    id: GO:0043025
    label: neuronal cell body
  evidence_type: IDA
  original_reference_id: PMID:30880001
  review:
    summary: 'LGG-1 localizes to neuronal cell bodies.

      '
    action: ACCEPT
    reason: 'Hill et al. demonstrated LGG-1 localization in neuronal cell bodies using
      fluorescent reporters. UniProt confirms expression in neurons including AIY
      interneurons and touch receptor neurons.

      '
    supported_by:
    - reference_id: PMID:30880001
      supporting_text: Epub 2019 Mar 14. Maturation and Clearance of 
        Autophagosomes in Neurons Depends on a Specific Cysteine Protease 
        Isoform, ATG-4.2.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:29255173
  review:
    summary: 'LGG-1 interacts with ALLO-1, the autophagy receptor for allophagy.

      '
    action: MODIFY
    reason: 'This is a functionally critical interaction. ALLO-1 is the autophagy
      receptor that mediates paternal organelle clearance by binding to LGG-1 via
      its LIR motif. "Protein binding" is too generic for this specific receptor-cargo
      adaptor interaction. A term capturing LIR-mediated binding would be more appropriate
      if available.

      '
    proposed_replacement_terms:
    - id: GO:0044877
      label: protein-containing complex binding
    supported_by:
    - reference_id: PMID:29255173
      supporting_text: ALLO-1 is essential for autophagosome formation around 
        paternal organelles and directly binds to the worm LC3 homologue LGG-1 
        through its LC3-interacting region (LIR) motif.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:29255173
  review:
    summary: 'LGG-1 localizes to cytoplasm.

      '
    action: ACCEPT
    reason: 'Confirmed by multiple studies. LGG-1 cycles between cytosolic and membrane-bound
      forms.

      '
    supported_by:
    - reference_id: PMID:29255173
      supporting_text: Dec 18. The autophagy receptor ALLO-1 and the IKKE-1 
        kinase control clearance of paternal mitochondria in Caenorhabditis 
        elegans.
- term:
    id: GO:2000786
    label: positive regulation of autophagosome assembly
  evidence_type: IMP
  original_reference_id: PMID:24374177
  review:
    summary: 'LGG-1 positively regulates autophagosome assembly.

      '
    action: ACCEPT
    reason: 'Manil-Segalen et al. demonstrated that LGG-1 is required for autophagosome
      formation and promotes assembly of LGG-2-positive autophagosomes. This is consistent
      with LGG-1''s role as an essential autophagosome biogenesis factor.

      '
    supported_by:
    - reference_id: PMID:24374177
      supporting_text: LGG-1 acts upstream of LGG-2 to allow its localization to
        autophagosomes
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: IDA
  original_reference_id: PMID:25896323
  review:
    summary: 'LGG-1 localizes to the mitochondrial outer membrane during mitophagy.

      '
    action: ACCEPT
    reason: 'Palikaras et al. demonstrated LGG-1 localization at mitochondria during
      mitophagy. This localization is consistent with autophagosome formation around
      mitochondria for degradation.

      '
    supported_by:
    - reference_id: PMID:25896323
      supporting_text: Impaired mitochondrial maintenance in disparate cell 
        types is a shared hallmark of many human pathologies and ageing
- term:
    id: GO:0050830
    label: defense response to Gram-positive bacterium
  evidence_type: IEP
  original_reference_id: PMID:24882217
  review:
    summary: 'LGG-1 is induced during defense against Gram-positive bacteria.

      '
    action: KEEP_AS_NON_CORE
    reason: 'The IEP evidence indicates expression induction during bacterial infection,
      not direct involvement. This is a downstream consequence of autophagy induction
      during innate immune responses rather than a core function.

      '
    supported_by:
    - reference_id: PMID:24882217
      supporting_text: 2014 May 29. Innate host defense requires TFEB-mediated 
        transcription of cytoprotective and antimicrobial genes.
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IDA
  original_reference_id: PMID:24882217
  review:
    summary: 'LGG-1 localizes to autophagosomes.

      '
    action: ACCEPT
    reason: 'Multiple IDA studies confirm autophagosome localization. This is a core
      characteristic of LGG-1 function.

      '
    supported_by:
    - reference_id: PMID:24882217
      supporting_text: 2014 May 29. Innate host defense requires TFEB-mediated 
        transcription of cytoprotective and antimicrobial genes.
- term:
    id: GO:0000421
    label: autophagosome membrane
  evidence_type: IDA
  original_reference_id: PMID:24374177
  review:
    summary: 'LGG-1 localizes to autophagosome membranes.

      '
    action: ACCEPT
    reason: 'Manil-Segalen et al. (PMID:24374177) demonstrated LGG-1 localization
      to autophagosome membranes using fluorescent reporters and EM.

      '
    supported_by:
    - reference_id: PMID:24374177
      supporting_text: 2013 Dec 26. The C. elegans LC3 acts downstream of 
        GABARAP to degrade autophagosomes by interacting with the HOPS subunit 
        VPS39.
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IDA
  original_reference_id: PMID:22560223
  review:
    summary: 'LGG-1 localizes to autophagosomes.

      '
    action: ACCEPT
    reason: 'Robida-Stubbs et al. used LGG-1 reporters to monitor autophagy in the
      context of TOR signaling and lifespan.

      '
    supported_by:
    - reference_id: PMID:22560223
      supporting_text: TOR signaling and rapamycin influence longevity by 
        regulating SKN-1/Nrf and DAF-16/FoxO.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: HDA
  original_reference_id: PMID:21611156
  review:
    summary: 'LGG-1 may localize to the nucleus based on high-throughput data.

      '
    action: UNDECIDED
    reason: 'This HDA annotation is based on proteome-wide localization studies in
      body wall muscle. Nuclear localization of LGG-1 is unexpected for an autophagy
      protein, and I cannot verify this claim. Recent nucleophagy studies from the
      deep research suggest possible nuclear-associated functions but direct nuclear
      localization requires more evidence.

      '
    supported_by:
    - reference_id: PMID:21611156
      supporting_text: Determining the sub-cellular localization of proteins 
        within Caenorhabditis elegans body wall muscle.
- term:
    id: GO:0008340
    label: determination of adult lifespan
  evidence_type: IGI
  original_reference_id: PMID:21906946
  review:
    summary: 'LGG-1 is required for lifespan extension in germline-less animals.

      '
    action: KEEP_AS_NON_CORE
    reason: 'Lapierre et al. (PMID:21906946) showed autophagy is required for longevity
      in germline-less animals. This is a pleiotropic consequence of autophagy function
      on aging rather than a primary LGG-1 function.

      '
    supported_by:
    - reference_id: PMID:21906946
      supporting_text: 2011 Sep 8. Autophagy and lipid metabolism coordinately 
        modulate life span in germline-less C.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:20523114
  review:
    summary: 'LGG-1 localizes to cytoplasm.

      '
    action: ACCEPT
    reason: 'Alberti et al. confirmed cytoplasmic localization of LGG-1 in studies
      of LGG-1/LGG-2 synergy during dauer formation.

      '
    supported_by:
    - reference_id: PMID:20523114
      supporting_text: The autophagosomal protein LGG-2 acts synergistically 
        with LGG-1 in dauer formation and longevity in C.
- term:
    id: GO:0012501
    label: programmed cell death
  evidence_type: IGI
  original_reference_id: PMID:17327275
  review:
    summary: 'LGG-1 contributes to programmed cell death in the context of neurodegeneration.

      '
    action: KEEP_AS_NON_CORE
    reason: 'Toth et al. showed that autophagy genes contribute to ion-channel-dependent
      neurodegeneration. This is a context-dependent phenotype rather than a core
      function. Inactivation of lgg-1 partially suppresses neuronal death.

      '
    supported_by:
    - reference_id: PMID:17327275
      supporting_text: Inactivation of unc-51, bec-1 and lgg-1, the worm 
        counterparts of the yeast autophagy genes Atg1, Atg6 and Atg8 
        respectively, partially suppresses degeneration of neurons with toxic 
        ion channel variants.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IDA
  original_reference_id: PMID:12958363
  review:
    summary: 'LGG-1 localizes to cytoplasm.

      '
    action: ACCEPT
    reason: 'The foundational autophagy paper in C. elegans confirmed cytoplasmic
      localization of LGG-1.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: Autophagy genes are essential for dauer development and 
        life-span extension in C.
- term:
    id: GO:0005776
    label: autophagosome
  evidence_type: IDA
  original_reference_id: PMID:12958363
  review:
    summary: 'LGG-1 localizes to autophagosomes.

      '
    action: ACCEPT
    reason: 'Melendez et al. established GFP::LGG-1 as the standard autophagosome
      marker in C. elegans.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: Dauer formation is associated with increased autophagy 
        and also requires C. elegans orthologs of the yeast autophagy genes 
        APG1, APG7, APG8, and AUT10
- term:
    id: GO:0006914
    label: autophagy
  evidence_type: IGI
  original_reference_id: PMID:12958363
  review:
    summary: 'LGG-1 is essential for autophagy.

      '
    action: ACCEPT
    reason: 'This is the core function. Melendez et al. established that lgg-1 (APG8
      ortholog) is essential for autophagy in C. elegans.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: autophagy genes are essential for dauer development and 
        life-span extension in C. elegans
- term:
    id: GO:0040024
    label: dauer larval development
  evidence_type: IGI
  original_reference_id: PMID:12958363
  review:
    summary: 'LGG-1 is required for dauer development.

      '
    action: ACCEPT
    reason: 'Dauer development requires functional autophagy, and LGG-1 is essential
      for this process. This was established in the foundational autophagy paper by
      Melendez et al. While dauer-related, this is a well-characterized developmental
      requirement for autophagy in C. elegans.

      '
    supported_by:
    - reference_id: PMID:12958363
      supporting_text: autophagy genes are essential for dauer development and 
        life-span extension in C. elegans
references:
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular 
    Location vocabulary mapping, accompanied by conservative changes to GO terms
    applied by UniProt
  findings: []
- id: PMID:12958363
  title: Autophagy genes are essential for dauer development and life-span 
    extension in C. elegans.
  findings:
  - statement: Established LGG-1/APG8 as essential for autophagy in C. elegans
    supporting_text: Dauer formation is associated with increased autophagy and 
      also requires C. elegans orthologs of the yeast autophagy genes APG1, 
      APG7, APG8, and AUT10.
  - statement: Required for dauer development and longevity
    supporting_text: autophagy genes are essential for dauer development and 
      life-span extension in C. elegans
  - statement: GFP::LGG-1 established as autophagosome marker
    supporting_text: Autophagy, through the sequestration and delivery of cargo 
      to the lysosomes, is the major route for degrading long-lived proteins and
      cytoplasmic organelles in eukaryotic cells.
- id: PMID:14704431
  title: A map of the interactome network of the metazoan C. elegans.
  findings:
  - statement: High-throughput interactome mapping identified LGG-1 interactions
    supporting_text: A map of the interactome network of the metazoan C. 
      elegans.
- id: PMID:17327275
  title: Influence of autophagy genes on ion-channel-dependent neuronal 
    degeneration in Caenorhabditis elegans.
  findings:
  - statement: LGG-1 contributes to necrotic neurodegeneration
    supporting_text: Influence of autophagy genes on ion-channel-dependent 
      neuronal degeneration in Caenorhabditis elegans.
  - statement: Inactivation partially suppresses neuronal death
    supporting_text: Influence of autophagy genes on ion-channel-dependent 
      neuronal degeneration in Caenorhabditis elegans.
- id: PMID:19123269
  title: Empirically controlled mapping of the Caenorhabditis elegans 
    protein-protein interactome network.
  findings:
  - statement: Controlled interactome mapping confirmed LGG-1 interactions
    supporting_text: Empirically controlled mapping of the Caenorhabditis 
      elegans protein-protein interactome network.
- id: PMID:19167332
  title: SEPA-1 mediates the specific recognition and degradation of P granule 
    components by autophagy in C. elegans.
  findings:
  - statement: LGG-1 directly binds SEPA-1 cargo receptor
    supporting_text: SEPA-1 mediates the specific recognition and degradation of
      P granule components by autophagy in C. elegans.
  - statement: Required for P granule degradation in somatic cells
    supporting_text: SEPA-1 mediates the specific recognition and degradation of
      P granule components by autophagy in C. elegans.
  - statement: Established selective autophagy mechanism
    supporting_text: SEPA-1 mediates the specific recognition and degradation of
      P granule components by autophagy in C. elegans.
- id: PMID:20523114
  title: The autophagosomal protein LGG-2 acts synergistically with LGG-1 in 
    dauer formation and longevity in C. elegans.
  findings:
  - statement: LGG-1 and LGG-2 have synergistic functions
    supporting_text: The autophagosomal protein LGG-2 acts synergistically with 
      LGG-1 in dauer formation and longevity in C. elegans.
  - statement: Both required for dauer and longevity
    supporting_text: The autophagosomal protein LGG-2 acts synergistically with 
      LGG-1 in dauer formation and longevity in C. elegans.
- id: PMID:21611156
  title: Determining the sub-cellular localization of proteins within 
    Caenorhabditis elegans body wall muscle.
  findings:
  - statement: Proteome-wide localization study
    supporting_text: Determining the sub-cellular localization of proteins 
      within Caenorhabditis elegans body wall muscle.
- id: PMID:21906946
  title: Autophagy and lipid metabolism coordinately modulate life span in 
    germline-less C. elegans.
  findings:
  - statement: Autophagy required for longevity in germline-less animals
    supporting_text: Autophagy and lipid metabolism coordinately modulate life 
      span in germline-less C. elegans.
  - statement: Link between autophagy and lipid metabolism
    supporting_text: Autophagy and lipid metabolism coordinately modulate life 
      span in germline-less C. elegans.
- id: PMID:22157748
  title: Endocytosis and intracellular trafficking contribute to necrotic 
    neurodegeneration in C. elegans.
  findings:
  - statement: Autophagy synergizes with endocytosis in necrosis
    supporting_text: Endocytosis and intracellular trafficking contribute to 
      necrotic neurodegeneration in C. elegans.
- id: PMID:22560223
  title: TOR signaling and rapamycin influence longevity by regulating SKN-1/Nrf
    and DAF-16/FoxO.
  findings:
  - statement: TOR regulation of autophagy and longevity
    supporting_text: TOR signaling and rapamycin influence longevity by 
      regulating SKN-1/Nrf and DAF-16/FoxO.
- id: PMID:23619095
  title: Autophagy modulates miRNA-mediated gene silencing and selectively 
    degrades AIN-1/GW182 in C. elegans.
  findings:
  - statement: LGG-1 interacts with AIN-1
    supporting_text: Autophagy modulates miRNA-mediated gene silencing and 
      selectively degrades AIN-1/GW182 in C. elegans.
  - statement: Autophagy regulates miRNA silencing
    supporting_text: Autophagy modulates miRNA-mediated gene silencing and 
      selectively degrades AIN-1/GW182 in C. elegans.
- id: PMID:24374177
  title: The C. elegans LC3 acts downstream of GABARAP to degrade autophagosomes
    by interacting with the HOPS subunit VPS39.
  findings:
  - statement: LGG-1 acts upstream of LGG-2
    supporting_text: The C. elegans LC3 acts downstream of GABARAP to degrade 
      autophagosomes by interacting with the HOPS subunit VPS39.
  - statement: LGG-1 required for LGG-2 recruitment to autophagosomes
    supporting_text: The C. elegans LC3 acts downstream of GABARAP to degrade 
      autophagosomes by interacting with the HOPS subunit VPS39.
  - statement: Established sequential roles of ATG8 paralogs
    supporting_text: The C. elegans LC3 acts downstream of GABARAP to degrade 
      autophagosomes by interacting with the HOPS subunit VPS39.
- id: PMID:24882217
  title: Innate host defense requires TFEB-mediated transcription of 
    cytoprotective and antimicrobial genes.
  findings:
  - statement: HLH-30/TFEB regulates autophagy
    supporting_text: Innate host defense requires TFEB-mediated transcription of
      cytoprotective and antimicrobial genes.
  - statement: LGG-1 induced during infection
    supporting_text: Innate host defense requires TFEB-mediated transcription of
      cytoprotective and antimicrobial genes.
- id: PMID:25896323
  title: Coordination of mitophagy and mitochondrial biogenesis during ageing in
    C. elegans.
  findings:
  - statement: LGG-1 required for mitophagy
    supporting_text: Coordination of mitophagy and mitochondrial biogenesis 
      during ageing in C. elegans.
  - statement: DCT-1 is key mitophagy mediator
    supporting_text: Coordination of mitophagy and mitochondrial biogenesis 
      during ageing in C. elegans.
  - statement: LGG-1 localizes to mitochondrial outer membrane
    supporting_text: Coordination of mitophagy and mitochondrial biogenesis 
      during ageing in C. elegans.
- id: PMID:26687600
  title: Structural Basis of the Differential Function of the Two C. elegans 
    Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.
  findings:
  - statement: Crystal structure of LGG-1
    supporting_text: Structural Basis of the Differential Function of the Two C.
      elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.
  - statement: LGG-1 binds LIR motifs in cargo receptors
    supporting_text: Structural Basis of the Differential Function of the Two C.
      elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.
  - statement: Direct interactions with SEPA-1, SQST-1, EPG-7, ATG-13, UNC-51
    supporting_text: Structural Basis of the Differential Function of the Two C.
      elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy.
- id: PMID:27875098
  title: HLH-30/TFEB-mediated autophagy functions in a cell-autonomous manner 
    for epithelium intrinsic cellular defense against bacterial pore-forming 
    toxin in C. elegans.
  findings:
  - statement: LGG-1 required for xenophagy of bacterial toxins
    supporting_text: HLH-30/TFEB-mediated autophagy functions in a 
      cell-autonomous manner for epithelium intrinsic cellular defense against 
      bacterial pore-forming toxin in C. elegans.
  - statement: Autophagy contributes to membrane pore repair
    supporting_text: HLH-30/TFEB-mediated autophagy functions in a 
      cell-autonomous manner for epithelium intrinsic cellular defense against 
      bacterial pore-forming toxin in C. elegans.
- id: PMID:28198373
  title: Hormetic heat stress and HSF-1 induce autophagy to improve survival and
    proteostasis in C. elegans.
  findings:
  - statement: LGG-1 induced by heat stress
    supporting_text: Hormetic heat stress and HSF-1 induce autophagy to improve 
      survival and proteostasis in C. elegans.
  - statement: Required for thermoresistance and longevity
    supporting_text: Hormetic heat stress and HSF-1 induce autophagy to improve 
      survival and proteostasis in C. elegans.
  - statement: Essential for hormetic heat shock benefits
    supporting_text: Hormetic heat stress and HSF-1 induce autophagy to improve 
      survival and proteostasis in C. elegans.
- id: PMID:29255173
  title: The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance 
    of paternal mitochondria in Caenorhabditis elegans.
  findings:
  - statement: LGG-1 binds ALLO-1 autophagy receptor via LIR
    supporting_text: The autophagy receptor ALLO-1 and the IKKE-1 kinase control
      clearance of paternal mitochondria in Caenorhabditis elegans.
  - statement: Required for paternal mitochondrial elimination
    supporting_text: The autophagy receptor ALLO-1 and the IKKE-1 kinase control
      clearance of paternal mitochondria in Caenorhabditis elegans.
- id: PMID:30880001
  title: Maturation and Clearance of Autophagosomes in Neurons Depends on a 
    Specific Cysteine Protease Isoform, ATG-4.2.
  findings:
  - statement: LGG-1 localization in neurons
    supporting_text: Maturation and Clearance of Autophagosomes in Neurons 
      Depends on a Specific Cysteine Protease Isoform, ATG-4.2.
  - statement: ATG-4.2 required for neuronal autophagy
    supporting_text: Maturation and Clearance of Autophagosomes in Neurons 
      Depends on a Specific Cysteine Protease Isoform, ATG-4.2.
- id: PMID:37395461
  title: LGG-1/GABARAP lipidation is not required for autophagy and development 
    in Caenorhabditis elegans.
  findings:
  - statement: C-terminal cleavage essential for autophagosome initiation
    supporting_text: LGG-1/GABARAP lipidation is not required for autophagy and 
      development in Caenorhabditis elegans.
  - statement: Lipidation not strictly required for autophagy
    supporting_text: LGG-1/GABARAP lipidation is not required for autophagy and 
      development in Caenorhabditis elegans.
  - statement: Lipidation enhances cargo recognition and LGG-2 formation
    supporting_text: LGG-1/GABARAP lipidation is not required for autophagy and 
      development in Caenorhabditis elegans.
- id: PMID:22767594
  title: Differential function of the two Atg4 homologues in the aggrephagy 
    pathway in Caenorhabditis elegans.
  findings:
  - statement: ATG-4.1 and ATG-4.2 process LGG-1
    supporting_text: Differential function of the two Atg4 homologues in the 
      aggrephagy pathway in Caenorhabditis elegans.
  - statement: Required for aggrephagy
    supporting_text: Differential function of the two Atg4 homologues in the 
      aggrephagy pathway in Caenorhabditis elegans.
- id: file:worm/lgg-1/lgg-1-deep-research-falcon.md
  title: Deep research summary for LGG-1 function
  findings:
  - statement: LGG-1 is the C. elegans ortholog of ATG8/LC3/GABARAP family
  - statement: Functions in autophagosome biogenesis and selective autophagy
  - statement: Participates in paternal mitochondrial elimination and 
      nucleophagy
core_functions:
- molecular_function:
    id: GO:0008429
    label: phosphatidylethanolamine binding
  description: 'LGG-1 is an ATG8 family ubiquitin-like modifier that is covalently
    conjugated to PE at Gly-116 through the ATG8 conjugation cascade (ATG4 cleavage,
    ATG7/ATG3 transfer). This lipidation anchors LGG-1 to autophagosomal membranes
    and is the core molecular function enabling autophagosome biogenesis.

    '
  directly_involved_in:
  - id: GO:0016236
    label: macroautophagy
  - id: GO:0000045
    label: autophagosome assembly
  locations:
  - id: GO:0000421
    label: autophagosome membrane
  - id: GO:0005776
    label: autophagosome
proposed_new_terms: []
suggested_questions:
- question: 'Does LGG-1 have any GABA receptor-related function in C. elegans neurons,
    or is the GABA receptor binding annotation purely a historical artifact from mammalian
    GABARAP nomenclature?

    '
suggested_experiments:
- description: 'Test LGG-1 interaction with GABA receptors (e.g., UNC-49) using co-immunoprecipitation
    or split-GFP assays to validate or refute the GABA receptor binding annotation.
    This would clarify whether GABARAP-like function extends to GABA receptor trafficking
    in C. elegans or if this is purely an autophagy protein.

    '
  hypothesis: 'LGG-1 does not directly interact with GABA receptors in C. elegans,
    and the GABA receptor binding annotation is a nomenclature artifact from mammalian
    GABARAP.

    '
tags:
- caeel-proteostasis
- caeel-mitophagy