FASLG

Summary: The ADAM10/SPPL2A-generated FasL intracellular domain can enter the nucleus and inhibit transcription.

Reason: This is a valid activity of a processed FASLG fragment, but it is separable from the core membrane-ligand cytokine activity that initiates FAS apoptosis.

Summary: FASLG binds the FAS/CD95 death receptor; the seeded term is broader than the supported receptor class.

Reason: FASLG is a TNF-family ligand whose informative binding activity is engagement of the FAS death receptor, not generic signaling-receptor or TNF-receptor-superfamily binding.

Proposed replacements: death receptor binding

Summary: FASLG binds the FAS/CD95 death receptor; the seeded term is broader than the supported receptor class.

Reason: FASLG is a TNF-family ligand whose informative binding activity is engagement of the FAS death receptor, not generic signaling-receptor or TNF-receptor-superfamily binding.

Proposed replacements: death receptor binding

Summary: FASLG binds the FAS/CD95 death receptor through its extracellular TNF-homology domain.

Reason: Death receptor binding is the precise molecular function for the FASLG:FAS ligand-receptor pair.

Summary: FASLG is a pro-apoptotic TNF-family cytokine that can trigger FAS-dependent death-receptor signaling.

Reason: Cytokine activity is the GO-CAM molecular-function choice for the extracellular FASLG ligand step and is supported by FASLG-dependent apoptosis assays.

Summary: FASLG is a pro-apoptotic TNF-family cytokine that can trigger FAS-dependent death-receptor signaling.

Reason: Cytokine activity is the GO-CAM molecular-function choice for the extracellular FASLG ligand step and is supported by FASLG-dependent apoptosis assays.

Summary: FASLG binds the FAS/CD95 death receptor; the seeded term is broader than the supported receptor class.

Reason: FASLG is a TNF-family ligand whose informative binding activity is engagement of the FAS death receptor, not generic signaling-receptor or TNF-receptor-superfamily binding.

Proposed replacements: death receptor binding

Summary: PMID:12198154 analyzes CASP10 recruitment to native CD95 and TRAIL DISCs, not a direct FASLG-CASP8 molecular function.

Reason: FASLG is the extracellular ligand that activates FAS; CASP8 is recruited cytosolically by FADD, so the imported generic protein-binding edge is indirect and should not stand as a FASLG molecular function.

Summary: PMID:12887920 is TNFR1-centered and the cached abstract does not expose the FASLG-specific IPI behind this row.

Reason: The annotation may come from a full-text comparison to CD95 signaling, but the local abstract is insufficient to verify the asserted FASLG partner edge.

Summary: PMID:12887920 is TNFR1-centered and the cached abstract does not expose the FASLG-specific IPI behind this row.

Reason: The annotation may come from a full-text comparison to CD95 signaling, but the local abstract is insufficient to verify the asserted FASLG partner edge.

Summary: PMID:12887920 is TNFR1-centered and the cached abstract does not expose the FASLG-specific IPI behind this row.

Reason: The annotation may come from a full-text comparison to CD95 signaling, but the local abstract is insufficient to verify the asserted FASLG partner edge.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: FCH/SH3 family proteins can associate with the FasL cytoplasmic tail and change FASLG intracellular localization.

Reason: The reported cytoplasmic-tail PPI is relevant to trafficking but leaves the row at uninformative generic protein binding and does not establish a FASLG molecular function more specific than the core FAS death-receptor ligand activity.

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: NCK1 binds the proline-rich FasL cytoplasmic tail and may guide FasL-positive secretory lysosomes.

Reason: The NCK1 edge is a trafficking adaptor interaction, not an informative stand-alone molecular function for FASLG.

Summary: The Schwann-cell proteomics paper identified FasL-associated trafficking/endocytosis proteins.

Reason: SNX18/AP2B1 associations describe candidate regulation of FasL trafficking and surface expression, not the extracellular death-receptor ligand activity curated as FASLG core function.

Summary: The Schwann-cell proteomics paper identified FasL-associated trafficking/endocytosis proteins.

Reason: SNX18/AP2B1 associations describe candidate regulation of FasL trafficking and surface expression, not the extracellular death-receptor ligand activity curated as FASLG core function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: This row comes from a phage-display survey of SH3 domains against the FasL cytoplasmic region.

Reason: The screen identifies candidate SH3-mediated interactions but the generic protein-binding term is uninformative and the row does not establish a distinct FASLG molecular function.

Summary: The cached PMID:21803845 abstract supports PMLRARalpha/FAS/c-FLIP complexes but does not verify a direct FASLG:FAS experiment.

Reason: Because the paper is abstract-only locally and appears focused on FAS inhibition in acute promyelocytic leukemia, this exact imported PPI needs a full-text check.

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: This endogenous HeLa interaction row comes from a broad proximity-ligation survey.

Reason: The PLA screen does not convert FASLG proximity to FAS, FADD, FYN, or PIK3R1 into a curated FASLG molecular function.

Summary: This endogenous HeLa interaction row comes from a broad proximity-ligation survey.

Reason: The PLA screen does not convert FASLG proximity to FAS, FADD, FYN, or PIK3R1 into a curated FASLG molecular function.

Summary: This endogenous HeLa interaction row comes from a broad proximity-ligation survey.

Reason: The PLA screen does not convert FASLG proximity to FAS, FADD, FYN, or PIK3R1 into a curated FASLG molecular function.

Summary: This endogenous HeLa interaction row comes from a broad proximity-ligation survey.

Reason: The PLA screen does not convert FASLG proximity to FAS, FADD, FYN, or PIK3R1 into a curated FASLG molecular function.

Summary: This row is a proteome-scale human interactome import.

Reason: Large binary interactome edges to RGS20, TRIP6, KRT40, or NOTCH2NLA are not evidence for FASLG death-receptor binding or a curated FasL-tail activity.

Summary: This row is a proteome-scale human interactome import.

Reason: Large binary interactome edges to RGS20, TRIP6, KRT40, or NOTCH2NLA are not evidence for FASLG death-receptor binding or a curated FasL-tail activity.

Summary: This row is a proteome-scale human interactome import.

Reason: Large binary interactome edges to RGS20, TRIP6, KRT40, or NOTCH2NLA are not evidence for FASLG death-receptor binding or a curated FasL-tail activity.

Summary: This row is a proteome-scale human interactome import.

Reason: Large binary interactome edges to RGS20, TRIP6, KRT40, or NOTCH2NLA are not evidence for FASLG death-receptor binding or a curated FasL-tail activity.

Summary: This row is a proteome-scale human interactome import.

Reason: Large binary interactome edges to RGS20, TRIP6, KRT40, or NOTCH2NLA are not evidence for FASLG death-receptor binding or a curated FasL-tail activity.

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: The NCK1 row comes from an alternative-splicing interactome screen rather than focused FASLG biology.

Reason: This high-throughput interaction is not an informative FASLG molecular function.

Summary: The SNX33 row comes from BioPlex AP-MS co-complex mapping.

Reason: A proteome-scale AP-MS edge in HEK293T cells does not establish a physiologic FASLG activity.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: This row is a HuRI yeast-two-hybrid interactome import.

Reason: These binary interactome hits do not establish an apoptosis-specific or trafficking-specific FASLG activity and should not remain as generic protein binding.

Summary: The SNX33 row comes from BioPlex 3.0 AP-MS co-complex mapping.

Reason: A proteome-scale AP-MS edge does not establish a curated FASLG molecular function.

Summary: The cited FASLG stimulation experiment supports the FASLG:FAS death-ligand interaction rather than a direct FASLG association with cytosolic DISC proteins.

Reason: These generic PPI imports are being narrowed to the direct receptor-binding activity that FASLG contributes upstream of FADD and CASP8 recruitment.

Proposed replacements: death receptor binding

Summary: This row comes from the 2025 U2OS multimodal cell-map AP-MS and imaging resource.

Reason: The SNX9/SNX33 cell-map edges are proteome-scale context data and do not justify generic protein-binding annotations on FASLG.

Summary: This row comes from the 2025 U2OS multimodal cell-map AP-MS and imaging resource.

Reason: The SNX9/SNX33 cell-map edges are proteome-scale context data and do not justify generic protein-binding annotations on FASLG.

Summary: FASLG has an extracellular receptor-binding ectodomain and can be released as soluble FasL.

Reason: The extracellular-region annotation is correct for the TNF-homology domain that binds FAS and for the soluble receptor-binding ectodomain.

Summary: FASLG has an extracellular receptor-binding ectodomain and can be released as soluble FasL.

Reason: The extracellular-region annotation is correct for the TNF-homology domain that binds FAS and for the soluble receptor-binding ectodomain.

Summary: FASLG has an extracellular receptor-binding ectodomain and can be released as soluble FasL.

Reason: The extracellular-region annotation is correct for the TNF-homology domain that binds FAS and for the soluble receptor-binding ectodomain.

Summary: FASLG has an extracellular receptor-binding ectodomain and can be released as soluble FasL.

Reason: The extracellular-region annotation is correct for the TNF-homology domain that binds FAS and for the soluble receptor-binding ectodomain.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: This Reactome event explicitly keeps FASLG in the extracellular FAS/CD95 receptor platform.

Reason: FASLG remains the extracellular ligand in the FAS receptor trimer and proximal FADD/procaspase recruitment events.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: True: entailed by extracellular exosome, kept in this review.

Reason: The claim is true: extracellular exosome, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: The processed FasL intracellular domain translocates to the nucleus.

Reason: Nuclear localization is valid for the SPPL2A-released ICD but is not the main extracellular ligand location of FASLG.

Summary: The processed FasL intracellular domain translocates to the nucleus.

Reason: Nuclear localization is valid for the SPPL2A-released ICD but is not the main extracellular ligand location of FASLG.

Summary: FASLG has an N-terminal cytoplasmic tail that can be liberated as the FasL ICD.

Reason: The cytoplasmic annotation is plausible for the membrane precursor and ICD, but it is ancillary to the extracellular TNF ligand function.

Summary: True: entailed by external side of plasma membrane, kept in this review.

Reason: The claim is true: external side of plasma membrane, kept in this review, entails this term. Other rows for this term are ACCEPTed. This row's reference does not establish it; that is recorded in source_defects, not grounds for REMOVE, which judges the claim.

Summary: Full-length FASLG is a type II plasma-membrane protein.

Reason: The membrane precursor places the receptor-binding TNF-homology domain outside the cell for FAS engagement.

Summary: Full-length FASLG is a type II plasma-membrane protein.

Reason: The membrane precursor places the receptor-binding TNF-homology domain outside the cell for FAS engagement.

Summary: Caveola is too specific for the well-supported human FASLG membrane/secretory-lysosome route.

Reason: This orthology-transferred location should not be treated as a core human FASLG localization without direct human evidence.

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: FASLG-dependent FAS signaling can eliminate activated immune and inflammatory cells.

Reason: This transferred immune-cell apoptosis context is plausible but is a cell-type outcome of the core FASLG death-receptor ligand activity.

Summary: Generic immune response is too broad for an InterPro TNF-family mapping.

Reason: FASLG participates in immune homeostasis through FAS-dependent cell death, but this parent process hides the direct death-receptor mechanism.

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: Positive regulation of proliferation is a noncanonical transferred outcome for FASLG.

Reason: FASLG can trigger non-apoptotic FAS outputs in some contexts, but this broad growth row should not be used as a core apoptosis annotation.

Summary: FASLG initiates extrinsic apoptotic signaling through the FAS/CD95 death receptor.

Reason: This is the canonical biological process for membrane FASLG and is the process used in the curated FASL-FAS GO-CAM.

Summary: FASLG initiates extrinsic apoptotic signaling through the FAS/CD95 death receptor.

Reason: This is the canonical biological process for membrane FASLG and is the process used in the curated FASL-FAS GO-CAM.

Summary: FASLG initiates extrinsic apoptotic signaling through the FAS/CD95 death receptor.

Reason: This is the canonical biological process for membrane FASLG and is the process used in the curated FASL-FAS GO-CAM.

Summary: FASLG initiates extrinsic apoptotic signaling through the FAS/CD95 death receptor.

Reason: This is the canonical biological process for membrane FASLG and is the process used in the curated FASL-FAS GO-CAM.

Summary: The full-length type II FASLG precursor is displayed at the external face of the cell membrane.

Reason: These membrane/cell-surface terms are correct, although less mechanistically informative than the FASLG cytokine activity.

Summary: The full-length type II FASLG precursor is displayed at the external face of the cell membrane.

Reason: These membrane/cell-surface terms are correct, although less mechanistically informative than the FASLG cytokine activity.

Summary: The full-length type II FASLG precursor is displayed at the external face of the cell membrane.

Reason: These membrane/cell-surface terms are correct, although less mechanistically informative than the FASLG cytokine activity.

Summary: FASLG can reduce angiogenesis indirectly by inducing endothelial-cell FAS apoptosis.

Reason: The anti-angiogenesis phenotype is downstream of soluble FasL-mediated endothelial apoptosis and should not be centered as a direct FASLG pathway step.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: The Ft1/PKB/GSK3/NF-ATc pathway controls production of FasL, whose death output is FAS-dependent extrinsic apoptosis.

Reason: If this expression-mediated row is retained on FASLG, it should be narrowed from generic positive regulation of apoptosis to the FAS death-receptor pathway executed by the FasL protein.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: FASLG can contribute to non-apoptotic FAS-dependent NF-kappaB signaling in some contexts.

Reason: NF-kappaB activation is not the core FASLG output, but FAS signaling can activate non-apoptotic transcriptional pathways, especially when the soluble ligand form or overexpression is used.

Summary: FASLG can contribute to non-apoptotic FAS-dependent NF-kappaB signaling in some contexts.

Reason: NF-kappaB activation is not the core FASLG output, but FAS signaling can activate non-apoptotic transcriptional pathways, especially when the soluble ligand form or overexpression is used.

Summary: FASLG traffics through secretory lysosomes before regulated surface delivery.

Reason: The lysosomal-lumen mapping captures storage of the FASLG ectodomain in FasL-positive secretory lysosomes.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: Endosomal lumen acidification is not a FASLG activity or localization.

Reason: This orthology-transferred row is too indirect and should not be retained for human FASLG.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: FASLG is stored in cytoplasmic vesicles/secretory lysosomes before cell-surface presentation.

Reason: The cytoplasmic vesicle lumen is a valid route for regulated FASLG trafficking in cytotoxic lymphocytes.

Summary: FASLG can be packaged in secreted exosome-like vesicles.

Reason: Extracellular vesicle FASLG is a supported but contextual extracellular delivery route rather than the core membrane FASLG:FAS platform.

Summary: Placental exosomal FasL contributes to T-cell suppression and lymphocyte apoptosis.

Reason: FASLG can kill T cells in specialized exosome-mediated immune-regulatory contexts, but this is a cell-type instance of FAS death-receptor signaling.

Summary: FAS stimulation can trigger RIPK-dependent caspase-independent necrotic death when caspases are blocked.

Reason: This is a noncanonical FASLG-dependent death branch, not the core CASP8 apoptotic pathway.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: This transferred context is not a direct human FASLG apoptosis step.

Reason: The row likely reflects a specific rat or contextual phenotype and overextends FASLG beyond death-receptor ligand biology.

Summary: PMID:11101870 is specifically about RIP-dependent non-apoptotic FAS death.

Reason: The better replacement is necroptotic signaling rather than apoptotic signaling because the paper tested FASLG-induced death in the absence of active caspases.

Proposed replacements: necroptotic signaling pathway

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: The source supports FAS death-receptor apoptosis more specifically than this broad signaling or apoptosis term.

Reason: Replace the generic process with the death-domain-receptor extrinsic apoptotic signaling pathway initiated by FASLG:FAS binding.

Proposed replacements: extrinsic apoptotic signaling pathway via death domain receptors

Summary: FAS stimulation can signal through a RIPK-dependent necroptotic branch when apoptotic caspase activity is absent.

Reason: Necroptotic signaling is a valid noncanonical FAS output but is not the core FASLG function.

Summary: ER calcium release is downstream type-II-cell signaling after FasL stimulation.

Reason: FASLG is the extracellular death ligand in PMID:26582200, but it does not itself release sequestered ER calcium.

Summary: FASLG was used as an apoptosis stimulus in a flippase-cleavage study.

Reason: Phosphatidylserine exposure is executed downstream by caspase-mediated control of lipid flippase/scramblase machinery, not by FASLG directly.

Summary: FASLG-mediated FAS activation can induce endothelial-cell apoptosis.

Reason: This cell-type-specific process is supported in endothelial cells but should not replace the broader FAS death-receptor pathway as the FASLG core.

Summary: FASLG binding activates FAS and positively regulates the downstream extrinsic apoptotic pathway.

Reason: As an extracellular ligand, FASLG acts upstream of the FAS receptor and directly turns on death-receptor extrinsic apoptotic signaling.

Summary: FASLG is the cognate TNF-family death ligand that initiates the Fas (CD95) signaling pathway by engaging trimeric FAS receptors at the plasma membrane.

Reason: FASLG directly performs the receptor-activating ligand step of the Fas signaling pathway (GO:0036337) by engaging and trimerizing cell-surface FAS/CD95 receptors through its extracellular TNF-homology domain to nucleate the FADD/CASP8 death-inducing signaling complex (PMID:7826947; PMID:9228058). Comparator death-receptor and cytokine ligands are annotated directly to their specific named receptor-signaling pathway terms (e.g. TNFSF10 on GO:0036462 TRAIL-activated apoptotic signaling pathway, IL34 on GO:0061514 interleukin-34-mediated signaling pathway, and C3 on GO:0002430 complement receptor mediated signaling pathway), and corroborating GO-CAM 663d668500001551 already places the downstream receptor and DISC components FAS (P25445), FADD (Q13158), and CASP8 (Q14790) in GO:0036337 while FASLG was annotated only to the broader parent GO:0008625 (extrinsic apoptotic signaling pathway via death domain receptors).