lgg-1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000045 autophagosome assembly	IBA GO_REF:0000033	ACCEPT	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). 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". Supporting Evidence: PMID:37395461 the cleavage of the C-terminus from the precursor is essential for the functionality of LGG-1(G116A) PMID:12958363 Dauer formation is associated with increased autophagy and also requires C. elegans orthologs of the yeast autophagy genes APG1, APG7, APG8, and AUT10.
GO:0000421 autophagosome membrane	IBA GO_REF:0000033	ACCEPT	Summary: LGG-1 localizes to autophagosome membranes through its lipidation with PE at Gly-116. This localization is conserved across ATG8 family proteins. 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." Supporting Evidence: PMID:24374177 The formation of the autophagic vesicles requires the recruitment of ubiquitin-like Atg8 proteins to the membrane of nascent autophagosomes. PMID:37395461 the lipidation of LGG-1 appears to be important for the coordination between cargo recognition and autophagosome biogenesis
GO:0000423 mitophagy	IBA GO_REF:0000033	ACCEPT	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. 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". Supporting Evidence: PMID:25896323 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 file:worm/lgg-1/lgg-1-deep-research-falcon.md paternal mitochondria are selectively recognized and engulfed by LGG-1-positive autophagosomes
GO:0008429 phosphatidylethanolamine binding	IBA GO_REF:0000033	ACCEPT	Summary: LGG-1 is covalently conjugated to PE at Gly-116, which is the biochemical basis for its membrane association during autophagy. 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. Supporting Evidence: file:worm/lgg-1/lgg-1-deep-research-falcon.md ATG8/LC3/GABARAP family of ubiquitin-like proteins that are covalently conjugated to the autophagosomal membrane lipid phosphatidylethanolamine (PE) during macroautophagy
GO:0097352 autophagosome maturation	IBA GO_REF:0000033	ACCEPT	Summary: LGG-1 functions in autophagosome maturation, acting upstream of LGG-2 and recruiting it to maturing autophagosomes. 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. Supporting Evidence: PMID:24374177 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
GO:0031625 ubiquitin protein ligase binding	IBA GO_REF:0000033	ACCEPT	Summary: This annotation refers to binding of ATG8-family proteins to E1/E2-like enzymes in the conjugation pathway (ATG7, ATG3). 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. Supporting Evidence: file:worm/lgg-1/lgg-1-deep-research-falcon.md ATG7 (E1-like) activates ATG8; ATG3 (E2-like) transfers it to PE on isolation membranes, with the ATG12-ATG5-ATG16 complex facilitating lipidation
GO:0050811 GABA receptor binding	IBA GO_REF:0000033	REMOVE	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. 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.
GO:0006995 cellular response to nitrogen starvation	IBA GO_REF:0000033	ACCEPT	Summary: Autophagy is induced by nutrient starvation including nitrogen starvation, and ATG8 family proteins are upregulated under these conditions. 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. Supporting Evidence: PMID:12958363 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.
GO:0000407 phagophore assembly site	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 localizes to the phagophore assembly site/preautophagosomal structure where autophagosomes are nucleated. 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. Supporting Evidence: file:worm/lgg-1/lgg-1-deep-research-falcon.md ATG8 dosage controls phagophore expansion and autophagosome size; the LGG-1 paralog executes analogous functions in worms to promote autophagosome membrane growth and maturation
GO:0000421 autophagosome membrane	IEA GO_REF:0000044	ACCEPT	Summary: Duplicate of the IBA annotation. LGG-1 localizes to autophagosome membranes. Reason: This is consistent with the IBA annotation and experimentally validated. Multiple IDA annotations confirm autophagosome membrane localization.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 is found in the cytoplasm in its unlipidated, soluble form. Reason: LGG-1 cycles between cytosolic (unlipidated) and membrane-bound (lipidated) forms. UniProt confirms cytoplasmic localization with multiple IDA evidence. Supporting Evidence: file:worm/lgg-1/lgg-1-deep-research-falcon.md LGG-1 cycles between diffuse cytosolic and punctate membrane-associated forms
GO:0005739 mitochondrion	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 localizes to mitochondria during mitophagy processes. 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. Supporting Evidence: PMID:25896323 We find that DCT-1 is a key mediator of mitophagy and longevity assurance under conditions of stress in C. elegans
GO:0005776 autophagosome	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 is a definitive marker of autophagosomes. 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." Supporting Evidence: file:worm/lgg-1/lgg-1-deep-research-falcon.md GFP::LGG-1 puncta mark forming autophagosomes
GO:0005886 plasma membrane	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 can localize to the plasma membrane, particularly the cell membrane. 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.
GO:0006914 autophagy	IEA GO_REF:0000043	ACCEPT	Summary: LGG-1 is a core autophagy protein. Reason: This is the parent term and is fully supported by extensive experimental evidence. LGG-1 is essential for autophagy in C. elegans. Supporting Evidence: PMID:12958363 autophagy genes are essential for dauer development and life-span extension in C. elegans
GO:0030425 dendrite	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 localizes to dendrites in neurons. 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.
GO:0030670 phagocytic vesicle membrane	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 localizes to phagosome membranes during LC3-associated phagocytosis-like processes. 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." Supporting Evidence: file:worm/lgg-1/lgg-1-deep-research-falcon.md LGG-1 and LGG-2 puncta transiently localize adjacent to phagosomes; marker entry indicates autophagosome-phagosome fusion events
GO:0031410 cytoplasmic vesicle	IEA GO_REF:0000043	ACCEPT	Summary: LGG-1 localizes to cytoplasmic vesicles (autophagosomes). Reason: Autophagosomes are cytoplasmic vesicles. This is a parent term that is appropriately general.
GO:0043202 lysosomal lumen	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 is delivered to the lysosomal lumen as part of autophagosome-lysosome fusion. 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. Supporting Evidence: PMID:24374177 LGG-2 controls the maturation of LGG-1-positive autophagosomes and facilitates the tethering with the lysosomes
GO:0043204 perikaryon	IEA GO_REF:0000044	ACCEPT	Summary: LGG-1 localizes to the neuronal cell body (perikaryon). Reason: UniProt confirms perikaryon localization based on neuronal studies (PMID:30880001). This is consistent with the IDA annotation for neuronal cell body.
GO:0005515 protein binding	IPI PMID:14704431 A map of the interactome network of the metazoan C. elegans.	MODIFY	Summary: LGG-1 interacts with ATG-4.1 based on C. elegans interactome mapping. 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 replacements: protein-containing complex binding Supporting Evidence: PMID:14704431 Jan 2. A map of the interactome network of the metazoan C.
GO:0005515 protein binding	IPI PMID:19123269 Empirically controlled mapping of the Caenorhabditis elegans...	MODIFY	Summary: LGG-1 interacts with ATG-4.1 based on controlled interactome mapping. Reason: Same as above - protein binding is too general. The interaction with ATG-4.1 is the proteolytic enzyme that processes LGG-1. Proposed replacements: protein-containing complex binding Supporting Evidence: PMID:19123269 Empirically controlled mapping of the Caenorhabditis elegans protein-protein interactome network.
GO:0005515 protein binding	IPI PMID:19167332 SEPA-1 mediates the specific recognition and degradation of ...	MODIFY	Summary: LGG-1 directly interacts with SEPA-1, the P granule autophagy receptor. 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 replacements: protein-containing complex binding Supporting Evidence: PMID:19167332 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. PMID:26687600 Structural Basis of the Differential Function of the Two C.
GO:0005515 protein binding	IPI PMID:23619095 Autophagy modulates miRNA-mediated gene silencing and select...	ACCEPT	Summary: LGG-1 interacts with AIN-1, a component of the miRNA-induced silencing complex. 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. Supporting Evidence: PMID:23619095 Autophagy modulates miRNA-mediated gene silencing and selectively degrades AIN-1/GW182 in C.
GO:0070266 necroptotic process	IGI PMID:22157748 Endocytosis and intracellular trafficking contribute to necr...	KEEP AS NON CORE	Summary: LGG-1 contributes to necrotic neurodegeneration in ion channel mutants. 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. Supporting Evidence: PMID:17327275 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. PMID:22157748 Endocytosis and intracellular trafficking contribute to necrotic neurodegeneration in C.
GO:0008340 determination of adult lifespan	IMP PMID:28198373 Hormetic heat stress and HSF-1 induce autophagy to improve s...	KEEP AS NON CORE	Summary: LGG-1 is required for lifespan extension by hormetic heat stress. 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. Supporting Evidence: PMID:28198373 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
GO:0009408 response to heat	IMP PMID:28198373 Hormetic heat stress and HSF-1 induce autophagy to improve s...	KEEP AS NON CORE	Summary: LGG-1 is induced by heat stress and required for heat stress resistance. 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. Supporting Evidence: PMID:28198373 heat shock increased autophagosome numbers with different kinetics in each of the examined tissues
GO:0016236 macroautophagy	IMP PMID:28198373 Hormetic heat stress and HSF-1 induce autophagy to improve s...	ACCEPT	Summary: LGG-1 is essential for macroautophagy. 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. Supporting Evidence: PMID:12958363 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. PMID:28198373 Hormetic heat stress and HSF-1 induce autophagy to improve survival and proteostasis in C.
GO:0001778 plasma membrane repair	IMP PMID:27875098 HLH-30/TFEB-mediated autophagy functions in a cell-autonomou...	KEEP AS NON CORE	Summary: LGG-1 contributes to plasma membrane repair after pore-forming toxin damage. 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. Supporting Evidence: PMID:27875098 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
GO:0097237 cellular response to toxic substance	IMP PMID:27875098 HLH-30/TFEB-mediated autophagy functions in a cell-autonomou...	KEEP AS NON CORE	Summary: LGG-1 is involved in defense against bacterial pore-forming toxins. 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. Supporting Evidence: PMID:27875098 bacterial membrane pore-forming toxin (PFT) induces autophagy in an HLH-30-dependent manner in Caenorhabditis elegans
GO:0098792 xenophagy	IMP PMID:27875098 HLH-30/TFEB-mediated autophagy functions in a cell-autonomou...	ACCEPT	Summary: LGG-1 is required for xenophagic degradation of bacterial toxins. 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. Supporting Evidence: PMID:27875098 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
GO:0043005 neuron projection	IDA PMID:30880001 Maturation and Clearance of Autophagosomes in Neurons Depend...	ACCEPT	Summary: LGG-1 localizes to neuron projections in AIY interneurons. Reason: Hill et al. (PMID:30880001) used fluorescent reporters to demonstrate LGG-1 localization in neuronal compartments including projections. UniProt confirms neuron projection localization. Supporting Evidence: PMID:30880001 Epub 2019 Mar 14. Maturation and Clearance of Autophagosomes in Neurons Depends on a Specific Cysteine Protease Isoform, ATG-4.2.
GO:0043025 neuronal cell body	IDA PMID:30880001 Maturation and Clearance of Autophagosomes in Neurons Depend...	ACCEPT	Summary: LGG-1 localizes to neuronal cell bodies. 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. Supporting Evidence: PMID:30880001 Epub 2019 Mar 14. Maturation and Clearance of Autophagosomes in Neurons Depends on a Specific Cysteine Protease Isoform, ATG-4.2.
GO:0005515 protein binding	IPI PMID:29255173 The autophagy receptor ALLO-1 and the IKKE-1 kinase control ...	MODIFY	Summary: LGG-1 interacts with ALLO-1, the autophagy receptor for allophagy. 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 replacements: protein-containing complex binding Supporting Evidence: PMID:29255173 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.
GO:0005737 cytoplasm	IDA PMID:29255173 The autophagy receptor ALLO-1 and the IKKE-1 kinase control ...	ACCEPT	Summary: LGG-1 localizes to cytoplasm. Reason: Confirmed by multiple studies. LGG-1 cycles between cytosolic and membrane-bound forms. Supporting Evidence: PMID:29255173 Dec 18. The autophagy receptor ALLO-1 and the IKKE-1 kinase control clearance of paternal mitochondria in Caenorhabditis elegans.
GO:2000786 positive regulation of autophagosome assembly	IMP PMID:24374177 The C. elegans LC3 acts downstream of GABARAP to degrade aut...	ACCEPT	Summary: LGG-1 positively regulates autophagosome assembly. 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. Supporting Evidence: PMID:24374177 LGG-1 acts upstream of LGG-2 to allow its localization to autophagosomes
GO:0005741 mitochondrial outer membrane	IDA PMID:25896323 Coordination of mitophagy and mitochondrial biogenesis durin...	ACCEPT	Summary: LGG-1 localizes to the mitochondrial outer membrane during mitophagy. Reason: Palikaras et al. demonstrated LGG-1 localization at mitochondria during mitophagy. This localization is consistent with autophagosome formation around mitochondria for degradation. Supporting Evidence: PMID:25896323 Impaired mitochondrial maintenance in disparate cell types is a shared hallmark of many human pathologies and ageing
GO:0050830 defense response to Gram-positive bacterium	IEP PMID:24882217 Innate host defense requires TFEB-mediated transcription of ...	KEEP AS NON CORE	Summary: LGG-1 is induced during defense against Gram-positive bacteria. 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. Supporting Evidence: PMID:24882217 2014 May 29. Innate host defense requires TFEB-mediated transcription of cytoprotective and antimicrobial genes.
GO:0005776 autophagosome	IDA PMID:24882217 Innate host defense requires TFEB-mediated transcription of ...	ACCEPT	Summary: LGG-1 localizes to autophagosomes. Reason: Multiple IDA studies confirm autophagosome localization. This is a core characteristic of LGG-1 function. Supporting Evidence: PMID:24882217 2014 May 29. Innate host defense requires TFEB-mediated transcription of cytoprotective and antimicrobial genes.
GO:0000421 autophagosome membrane	IDA PMID:24374177 The C. elegans LC3 acts downstream of GABARAP to degrade aut...	ACCEPT	Summary: LGG-1 localizes to autophagosome membranes. Reason: Manil-Segalen et al. (PMID:24374177) demonstrated LGG-1 localization to autophagosome membranes using fluorescent reporters and EM. Supporting Evidence: PMID:24374177 2013 Dec 26. The C. elegans LC3 acts downstream of GABARAP to degrade autophagosomes by interacting with the HOPS subunit VPS39.
GO:0005776 autophagosome	IDA PMID:22560223 TOR signaling and rapamycin influence longevity by regulatin...	ACCEPT	Summary: LGG-1 localizes to autophagosomes. Reason: Robida-Stubbs et al. used LGG-1 reporters to monitor autophagy in the context of TOR signaling and lifespan. Supporting Evidence: PMID:22560223 TOR signaling and rapamycin influence longevity by regulating SKN-1/Nrf and DAF-16/FoxO.
GO:0005634 nucleus	HDA PMID:21611156 Determining the sub-cellular localization of proteins within...	UNDECIDED	Summary: LGG-1 may localize to the nucleus based on high-throughput data. 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. Supporting Evidence: PMID:21611156 Determining the sub-cellular localization of proteins within Caenorhabditis elegans body wall muscle.
GO:0008340 determination of adult lifespan	IGI PMID:21906946 Autophagy and lipid metabolism coordinately modulate life sp...	KEEP AS NON CORE	Summary: LGG-1 is required for lifespan extension in germline-less animals. 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. Supporting Evidence: PMID:21906946 2011 Sep 8. Autophagy and lipid metabolism coordinately modulate life span in germline-less C.
GO:0005737 cytoplasm	IDA PMID:20523114 The autophagosomal protein LGG-2 acts synergistically with L...	ACCEPT	Summary: LGG-1 localizes to cytoplasm. Reason: Alberti et al. confirmed cytoplasmic localization of LGG-1 in studies of LGG-1/LGG-2 synergy during dauer formation. Supporting Evidence: PMID:20523114 The autophagosomal protein LGG-2 acts synergistically with LGG-1 in dauer formation and longevity in C.
GO:0012501 programmed cell death	IGI PMID:17327275 Influence of autophagy genes on ion-channel-dependent neuron...	KEEP AS NON CORE	Summary: LGG-1 contributes to programmed cell death in the context of neurodegeneration. 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. Supporting Evidence: PMID:17327275 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.
GO:0005737 cytoplasm	IDA PMID:12958363 Autophagy genes are essential for dauer development and life...	ACCEPT	Summary: LGG-1 localizes to cytoplasm. Reason: The foundational autophagy paper in C. elegans confirmed cytoplasmic localization of LGG-1. Supporting Evidence: PMID:12958363 Autophagy genes are essential for dauer development and life-span extension in C.
GO:0005776 autophagosome	IDA PMID:12958363 Autophagy genes are essential for dauer development and life...	ACCEPT	Summary: LGG-1 localizes to autophagosomes. Reason: Melendez et al. established GFP::LGG-1 as the standard autophagosome marker in C. elegans. Supporting Evidence: PMID:12958363 Dauer formation is associated with increased autophagy and also requires C. elegans orthologs of the yeast autophagy genes APG1, APG7, APG8, and AUT10
GO:0006914 autophagy	IGI PMID:12958363 Autophagy genes are essential for dauer development and life...	ACCEPT	Summary: LGG-1 is essential for autophagy. Reason: This is the core function. Melendez et al. established that lgg-1 (APG8 ortholog) is essential for autophagy in C. elegans. Supporting Evidence: PMID:12958363 autophagy genes are essential for dauer development and life-span extension in C. elegans
GO:0040024 dauer larval development	IGI PMID:12958363 Autophagy genes are essential for dauer development and life...	ACCEPT	Summary: LGG-1 is required for dauer development. 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. Supporting Evidence: PMID:12958363 autophagy genes are essential for dauer development and life-span extension in C. elegans

Gene Description

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Core Functions

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.

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