{"gene":"MPZL2","run_date":"2026-06-10T02:59:51","timeline":{"discoveries":[{"year":1998,"finding":"MPZL2 (EVA/EVA1) encodes a novel immunoglobulin superfamily member expressed in thymus epithelium that mediates homophilic cell-cell adhesion and is poorly soluble in nonionic detergents, strongly suggesting cytoskeletal association. Its selective downregulation by T cell maturation and homophilic adhesion capacity implicate it in thymus organogenesis.","method":"RNA fingerprinting, expression analysis in thymus-derived epithelial cell lines, detergent solubility fractionation, cell adhesion assay","journal":"The Journal of cell biology","confidence":"Medium","confidence_rationale":"Tier 2/3 / Moderate — homophilic adhesion assay and biochemical fractionation in a single lab, multiple methods but no structural or mutagenesis validation","pmids":["9585423"],"is_preprint":false},{"year":1998,"finding":"Eva (MPZL2) transcripts are detected in spongiotrophoblast cells and early postimplantation decidua during mouse placentation, with expression restricted to invasive glycogen cells after day 11.5 p.c., suggesting a role for the adhesion molecule in trophoblast invasion and decidual interaction.","method":"In situ hybridization on mouse placentas from day 5.5 to 18.5 p.c.","journal":"Developmental genetics","confidence":"Low","confidence_rationale":"Tier 3 / Weak — localization by in situ hybridization in a single study, no functional loss-of-function experiment performed","pmids":["9883583"],"is_preprint":false},{"year":2007,"finding":"Transgenic overexpression of EVA (MPZL2) in the thymus cortex resulted in a modified stromal environment with increased organ size and absolute thymocyte cell number, while EVA is expressed in both fetal thymic epithelia and T cell precursors during early thymus organogenesis, indicating a role for EVA in structural organisation of the thymus.","method":"Transgenic mouse overexpression, histological and flow cytometric analysis","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — genetic gain-of-function in mouse with defined cellular phenotype, single lab","pmids":["17362876"],"is_preprint":false},{"year":2009,"finding":"Knockdown of Eva1 (MPZL2) in fetal liver-derived hematopoietic progenitors using RNA interference caused a delayed DN1-DN3 thymocyte transition and failure to generate CD4+CD8+ double-positive T cells in OP9-DL1 co-culture, and resulted in ~10-fold reduction in thymus reconstitution when transplanted into Rag2-γc double knockout mice, establishing a cell-autonomous requirement for EVA1 in early T lymphocyte development.","method":"RNAi knockdown in hematopoietic progenitors, OP9-DL1 co-culture, Rag2-γc DKO reconstitution, flow cytometry","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function with defined cellular phenotype in both in vitro and in vivo models, single lab","pmids":["19851463"],"is_preprint":false},{"year":2015,"finding":"Eva1 (MPZL2) is required for glioblastoma-initiating cell (GIC) self-renewal and tumor formation; mechanistically, Eva1 activates the RelB-dependent noncanonical NF-κB signaling pathway by recruiting TRAF2 to its cytoplasmic tail, thereby promoting GIC proliferation and stemness gene expression.","method":"Knockdown and overexpression in GICs, self-renewal/tumor-forming assays, co-immunoprecipitation of TRAF2, NF-κB pathway reporter/western blot analysis","journal":"Cancer research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP identifying TRAF2 recruitment plus loss/gain-of-function with defined pathway readout, single lab with multiple orthogonal methods","pmids":["26677976"],"is_preprint":false},{"year":2016,"finding":"EVA1 (MPZL2) physically interacts with CLCA2 via their transmembrane segments, co-localizes with E-cadherin at cell-cell junctions, and is required for mammary epithelial differentiation; knockdown of EVA1 in immortalized human mammary epithelial cells causes epithelial-to-mesenchymal transition (EMT). EVA1 also participates in a complex with CLCA2 and ZO-1.","method":"Membrane dihybrid screening, co-immunoprecipitation, deletion analysis of interacting domains, siRNA knockdown with EMT phenotypic readout, immunofluorescence co-localization","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and deletion mapping of interaction domain, combined with KD phenotype and co-localization, single lab","pmids":["26930581"],"is_preprint":false},{"year":2018,"finding":"Loss-of-function variants in MPZL2 cause autosomal recessive nonsyndromic sensorineural hearing loss. In Mpzl2-mutant mice, there is early-onset progressive sensorineural hearing impairment with histological evidence of altered outer hair cell and supporting cell organization, degeneration of the organ of Corti, and degeneration of spiral ganglion neurons, establishing that MPZL2-mediated cell adhesion is essential for structural integrity of the inner ear epithelium.","method":"Homozygosity mapping, whole-exome sequencing, audiometric evaluation of Mpzl2-mutant mice, histological analysis of cochlea","journal":"American journal of human genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — human genetics combined with mouse knockout audiometry and cochlear histology, independently replicated across multiple families","pmids":["29961571"],"is_preprint":false},{"year":2018,"finding":"The MPZL2 protein localizes to auditory inner and outer hair cells in the mouse inner ear with an asymmetric subcellular distribution, as determined by immunolocalization in wild-type mouse cochlear tissue.","method":"Immunolocalization/immunofluorescence in mouse inner ear sections","journal":"Human genetics","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct subcellular localization experiment in tissue, reported in a second independent study corroborating inner ear expression","pmids":["29982980"],"is_preprint":false},{"year":2023,"finding":"EVA1A (MPZL2/EVA1) is a lysosome- and endoplasmic reticulum-associated protein that promotes endothelial cell apoptosis and inflammatory activation under proatherogenic disturbed flow. Mechanistically, EVA1A suppresses autophagy under disturbed flow conditions; its knockdown promotes autophagic flux and reduces EC apoptosis. EVA1A expression is transcriptionally regulated by TWIST1 in a flow-direction-dependent manner. In vivo knockdown of the EVA1A orthologue in zebrafish reduced EC apoptosis.","method":"siRNA knockdown in human ECs, morpholino knockdown in zebrafish, autophagic flux assay (bafilomycin/LC3-II/p62), flow chamber experiments, zebrafish in vivo validation, ChIP/transcription factor analysis","journal":"Arteriosclerosis, thrombosis, and vascular biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (in vitro KD, autophagic flux assay, in vivo zebrafish KD), mechanistic pathway placement via TWIST1 and autophagy regulators, replicated across species","pmids":["36794585"],"is_preprint":false},{"year":2025,"finding":"Eva1 (MPZL2) is expressed in macrophages and plays a role in LPS-induced inflammatory responses, possibly through direct interaction with TLR4. Macrophage-specific Eva1 is the key mediator of obesity-induced visceral adipose dysfunction; transplantation of wild-type macrophages into whole-body Eva1 knockout mice abolished the metabolic protection, establishing macrophage-derived Eva1 as the functionally relevant source.","method":"Whole-body and adipocyte-specific Eva1 knockout mice, HFD model, macrophage transplantation, co-immunoprecipitation (TLR4 interaction), histological and transcriptomic analysis of adipose tissue","journal":"Metabolism: clinical and experimental","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic KO with macrophage reconstitution establishing cell-type specificity, plus Co-IP suggesting TLR4 interaction; single lab","pmids":["40118448"],"is_preprint":false},{"year":2025,"finding":"AAV-delivered PAM-flexible adenine base editor (ABE8eWQ-SpRY) correcting the homozygous c.220C>T (p.Q74X) mutation in a humanized Mpzl2 mouse model significantly restored hearing function, improved cochlear structural integrity, and reversed altered gene expression, demonstrating that restoration of MPZL2 function is sufficient to rescue the hearing loss phenotype.","method":"Humanized knock-in mouse model (hMPZL2Q74X/Q74X), dual-AAV delivery of base editor, ABR audiometry, cochlear histology, RNA-seq","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in vivo gene correction with structural, functional, and transcriptomic validation in a humanized model; single lab but multiple orthogonal readouts","pmids":["40764318"],"is_preprint":false}],"current_model":"MPZL2 (EVA1) is an immunoglobulin superfamily adhesion molecule that mediates homophilic cell-cell interactions at epithelial junctions; it is essential for structural integrity of the inner ear organ of Corti (loss causes progressive sensorineural hearing loss in humans and mice), regulates early thymocyte development through epithelial-haematopoietic crosstalk, promotes glioblastoma-initiating cell stemness via TRAF2-dependent noncanonical NF-κB activation, suppresses protective autophagy in endothelial cells under proatherogenic disturbed flow downstream of TWIST1, and mediates macrophage-driven visceral adipose inflammation possibly through TLR4 interaction."},"narrative":{"mechanistic_narrative":"MPZL2 (EVA/EVA1) is an immunoglobulin superfamily transmembrane protein that mediates homophilic cell-cell adhesion and associates with the cytoskeleton, functioning to organize epithelial architecture and tissue integrity [PMID:9585423]. At epithelial cell-cell junctions it co-localizes with E-cadherin and assembles into a complex with CLCA2 (bound through its transmembrane segment) and ZO-1, and its loss in mammary epithelial cells triggers epithelial-to-mesenchymal transition, marking it as a maintainer of the differentiated epithelial state [PMID:26930581]. In the inner ear, MPZL2 localizes to auditory hair cells [PMID:29982980], and loss-of-function variants cause autosomal recessive nonsyndromic sensorineural hearing loss; mutant mice show progressive hearing impairment with disorganization and degeneration of the organ of Corti and spiral ganglion neurons, establishing that MPZL2-mediated adhesion is essential for cochlear structural integrity [PMID:29961571]. Restoration of MPZL2 function by in vivo base editing of a humanized mutant allele rescues hearing and cochlear structure, demonstrating the phenotype is directly attributable to MPZL2 loss [PMID:40764318]. Beyond adhesion, MPZL2 has cell-type-specific signaling roles: it is required for early thymocyte development and thymus organization through epithelial-haematopoietic crosstalk [PMID:17362876, PMID:19851463], it promotes glioblastoma-initiating cell self-renewal by recruiting TRAF2 to its cytoplasmic tail to activate RelB-dependent noncanonical NF-κB signaling [PMID:26677976], it suppresses protective autophagy in endothelial cells under proatherogenic disturbed flow downstream of TWIST1 [PMID:36794585], and macrophage-derived MPZL2 drives obesity-induced visceral adipose inflammation in conjunction with a TLR4 interaction [PMID:40118448].","teleology":[{"year":1998,"claim":"Established MPZL2 as a novel immunoglobulin superfamily molecule capable of homophilic adhesion and cytoskeletal association, framing it as a candidate organizer of thymic epithelial structure.","evidence":"RNA fingerprinting, expression analysis in thymic epithelial lines, detergent fractionation, and cell adhesion assay","pmids":["9585423"],"confidence":"Medium","gaps":["No structural model or adhesion-interface mutagenesis","Binding partner mediating adhesion not identified","Cytoskeletal linkage inferred from solubility, not a defined interaction"]},{"year":1998,"claim":"Mapped MPZL2 expression to spongiotrophoblast and invasive glycogen cells during placentation, raising the possibility of a role in trophoblast invasion.","evidence":"In situ hybridization across mouse placental development","pmids":["9883583"],"confidence":"Low","gaps":["Expression only; no loss-of-function test of placental function","No mechanistic link to adhesion activity established"]},{"year":2007,"claim":"Showed that gain of MPZL2 in the thymic cortex enlarges the stromal compartment and increases thymocyte numbers, supporting a structural-organizational role in thymus development.","evidence":"Transgenic mouse overexpression with histology and flow cytometry","pmids":["17362876"],"confidence":"Medium","gaps":["Gain-of-function only; does not define the requirement","Molecular mechanism linking adhesion to stromal expansion unresolved"]},{"year":2009,"claim":"Demonstrated a cell-autonomous requirement for MPZL2 in early T lymphocyte development, advancing from correlation to functional necessity.","evidence":"RNAi knockdown in hematopoietic progenitors, OP9-DL1 co-culture, and Rag2-γc DKO reconstitution with flow cytometry","pmids":["19851463"],"confidence":"Medium","gaps":["Signaling pathway downstream of MPZL2 in thymocytes not defined","Adhesion partner driving the DN1-DN3 transition unknown"]},{"year":2015,"claim":"Identified a signaling output for MPZL2 by showing it recruits TRAF2 to its cytoplasmic tail to drive noncanonical NF-κB activation supporting glioblastoma stem cell self-renewal, extending its role beyond passive adhesion.","evidence":"Knockdown/overexpression in glioblastoma-initiating cells, TRAF2 co-immunoprecipitation, NF-κB reporter and western blot","pmids":["26677976"],"confidence":"Medium","gaps":["Cytoplasmic motif mediating TRAF2 binding not mapped","Whether this pathway operates in normal epithelia untested","Upstream ligand/adhesion event triggering signaling unknown"]},{"year":2016,"claim":"Placed MPZL2 in a defined junctional complex with CLCA2 and ZO-1 alongside E-cadherin and showed its loss drives EMT, mechanistically tying it to maintenance of the epithelial state.","evidence":"Membrane dihybrid screen, reciprocal co-IP with transmembrane deletion mapping, siRNA with EMT readout, immunofluorescence co-localization","pmids":["26930581"],"confidence":"Medium","gaps":["Functional consequence of CLCA2 binding for adhesion not dissected","Connection between junctional complex and EMT signaling unresolved"]},{"year":2018,"claim":"Established MPZL2 as a Mendelian deafness gene and showed its adhesion function is essential for cochlear structural integrity, with hair-cell localization supporting the site of action.","evidence":"Homozygosity mapping and exome sequencing in families, Mpzl2-mutant mouse audiometry and cochlear histology, plus immunolocalization to inner ear hair cells","pmids":["29961571","29982980"],"confidence":"High","gaps":["Adhesion partner in the organ of Corti not identified","Why degeneration is progressive rather than developmental unclear"]},{"year":2023,"claim":"Revealed a non-adhesion, organelle-associated role in which MPZL2 suppresses protective autophagy and promotes endothelial apoptosis under disturbed flow, placing it downstream of TWIST1 in a flow-dependent atherogenic circuit.","evidence":"siRNA in human ECs, autophagic flux assays, flow chamber, ChIP/TF analysis, and zebrafish morpholino knockdown","pmids":["36794585"],"confidence":"High","gaps":["Molecular mechanism by which MPZL2 inhibits autophagy not defined","Relationship between adhesion role and autophagy suppression unresolved"]},{"year":2025,"claim":"Defined macrophage-derived MPZL2 as the functionally relevant driver of obesity-induced visceral adipose inflammation, with a TLR4 interaction as candidate mechanism.","evidence":"Whole-body and adipocyte-specific knockout mice, HFD model, macrophage transplantation rescue, and TLR4 co-immunoprecipitation","pmids":["40118448"],"confidence":"Medium","gaps":["TLR4 interaction shown by Co-IP only, not reciprocally validated functionally","Whether MPZL2 modulates TLR4 signaling output directly untested"]},{"year":2025,"claim":"Demonstrated that restoring MPZL2 function is sufficient to reverse hearing loss, confirming the gene's causal role and establishing therapeutic tractability.","evidence":"Dual-AAV adenine base editor correction of c.220C>T in a humanized Mpzl2 knock-in mouse with ABR audiometry, cochlear histology, and RNA-seq","pmids":["40764318"],"confidence":"High","gaps":["Durability and developmental timing window of rescue not fully defined","Does not resolve the molecular adhesion mechanism in the cochlea"]},{"year":null,"claim":"The unifying biochemical mechanism connecting MPZL2's homophilic adhesion to its diverse signaling outputs (TRAF2/NF-κB, autophagy suppression, TLR4) remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structure of the adhesion interface or cytoplasmic signaling motifs","The physiological homophilic/heterophilic ligand in each tissue is undefined","Whether adhesion and signaling roles are separable functions is untested"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098631","term_label":"cell adhesion mediator activity","supporting_discovery_ids":[0,5,6]},{"term_id":"GO:0060089","term_label":"molecular transducer activity","supporting_discovery_ids":[4]}],"localization":[{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[0,5,7]},{"term_id":"GO:0005764","term_label":"lysosome","supporting_discovery_ids":[8]},{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[8]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[4]},{"term_id":"R-HSA-9612973","term_label":"Autophagy","supporting_discovery_ids":[8]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[2,3,6]}],"complexes":["CLCA2-ZO-1 junctional complex"],"partners":["CLCA2","ZO-1","TRAF2","TLR4"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O60487","full_name":"Myelin protein zero-like protein 2","aliases":["Epithelial V-like antigen 1"],"length_aa":215,"mass_kda":24.5,"function":"Mediates homophilic cell-cell adhesion","subcellular_location":"Membrane","url":"https://www.uniprot.org/uniprotkb/O60487/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/MPZL2","classification":"Not Classified","n_dependent_lines":3,"n_total_lines":1208,"dependency_fraction":0.0024834437086092716},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/MPZL2","total_profiled":1310},"omim":[{"mim_id":"618145","title":"DEAFNESS, AUTOSOMAL RECESSIVE 111; DFNB111","url":"https://www.omim.org/entry/618145"},{"mim_id":"611707","title":"MYELIN PROTEIN ZERO-LIKE 3; MPZL3","url":"https://www.omim.org/entry/611707"},{"mim_id":"605686","title":"CELL ADHESION MOLECULE 1; CADM1","url":"https://www.omim.org/entry/605686"},{"mim_id":"604873","title":"MYELIN PROTEIN ZERO-LIKE 2; MPZL2","url":"https://www.omim.org/entry/604873"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Cell Junctions","reliability":"Approved"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"esophagus","ntpm":208.1},{"tissue":"urinary bladder","ntpm":145.5}],"url":"https://www.proteinatlas.org/search/MPZL2"},"hgnc":{"alias_symbol":["EVA"],"prev_symbol":["EVA1"]},"alphafold":{"accession":"O60487","domains":[{"cath_id":"2.60.40.10","chopping":"24-146","consensus_level":"high","plddt":93.1667,"start":24,"end":146},{"cath_id":"1.20.5","chopping":"149-215","consensus_level":"medium","plddt":90.433,"start":149,"end":215}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O60487","model_url":"https://alphafold.ebi.ac.uk/files/AF-O60487-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O60487-F1-predicted_aligned_error_v6.png","plddt_mean":89.38},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=MPZL2","jax_strain_url":"https://www.jax.org/strain/search?query=MPZL2"},"sequence":{"accession":"O60487","fasta_url":"https://rest.uniprot.org/uniprotkb/O60487.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O60487/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O60487"}},"corpus_meta":[{"pmid":"11037017","id":"PMC_11037017","title":"Cognitive 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Etude du Vieillissement Artériel.","date":"2000","source":"Journal of the American Geriatrics Society","url":"https://pubmed.ncbi.nlm.nih.gov/11037017","citation_count":218,"is_preprint":false},{"pmid":"11751240","id":"PMC_11751240","title":"EVA: continuous automatic evaluation of protein structure prediction servers.","date":"2001","source":"Bioinformatics (Oxford, England)","url":"https://pubmed.ncbi.nlm.nih.gov/11751240","citation_count":133,"is_preprint":false},{"pmid":"23162105","id":"PMC_23162105","title":"Imaging work-up for screening of paraganglioma and pheochromocytoma in SDHx mutation carriers: a multicenter prospective study from the PGL.EVA Investigators.","date":"2012","source":"The Journal of clinical endocrinology and metabolism","url":"https://pubmed.ncbi.nlm.nih.gov/23162105","citation_count":121,"is_preprint":false},{"pmid":"12824315","id":"PMC_12824315","title":"EVA: Evaluation of protein structure prediction servers.","date":"2003","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/12824315","citation_count":119,"is_preprint":false},{"pmid":"19017801","id":"PMC_19017801","title":"Functional assessment of allelic variants in the SLC26A4 gene involved in Pendred syndrome and nonsyndromic EVA.","date":"2008","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/19017801","citation_count":90,"is_preprint":false},{"pmid":"9180247","id":"PMC_9180247","title":"Aging of the vascular wall: serum concentration of elastin peptides and elastase inhibitors in relation to cardiovascular risk factors. 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Its selective downregulation by T cell maturation and homophilic adhesion capacity implicate it in thymus organogenesis.\",\n      \"method\": \"RNA fingerprinting, expression analysis in thymus-derived epithelial cell lines, detergent solubility fractionation, cell adhesion assay\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2/3 / Moderate — homophilic adhesion assay and biochemical fractionation in a single lab, multiple methods but no structural or mutagenesis validation\",\n      \"pmids\": [\"9585423\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1998,\n      \"finding\": \"Eva (MPZL2) transcripts are detected in spongiotrophoblast cells and early postimplantation decidua during mouse placentation, with expression restricted to invasive glycogen cells after day 11.5 p.c., suggesting a role for the adhesion molecule in trophoblast invasion and decidual interaction.\",\n      \"method\": \"In situ hybridization on mouse placentas from day 5.5 to 18.5 p.c.\",\n      \"journal\": \"Developmental genetics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — localization by in situ hybridization in a single study, no functional loss-of-function experiment performed\",\n      \"pmids\": [\"9883583\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2007,\n      \"finding\": \"Transgenic overexpression of EVA (MPZL2) in the thymus cortex resulted in a modified stromal environment with increased organ size and absolute thymocyte cell number, while EVA is expressed in both fetal thymic epithelia and T cell precursors during early thymus organogenesis, indicating a role for EVA in structural organisation of the thymus.\",\n      \"method\": \"Transgenic mouse overexpression, histological and flow cytometric analysis\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — genetic gain-of-function in mouse with defined cellular phenotype, single lab\",\n      \"pmids\": [\"17362876\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"Knockdown of Eva1 (MPZL2) in fetal liver-derived hematopoietic progenitors using RNA interference caused a delayed DN1-DN3 thymocyte transition and failure to generate CD4+CD8+ double-positive T cells in OP9-DL1 co-culture, and resulted in ~10-fold reduction in thymus reconstitution when transplanted into Rag2-γc double knockout mice, establishing a cell-autonomous requirement for EVA1 in early T lymphocyte development.\",\n      \"method\": \"RNAi knockdown in hematopoietic progenitors, OP9-DL1 co-culture, Rag2-γc DKO reconstitution, flow cytometry\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function with defined cellular phenotype in both in vitro and in vivo models, single lab\",\n      \"pmids\": [\"19851463\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Eva1 (MPZL2) is required for glioblastoma-initiating cell (GIC) self-renewal and tumor formation; mechanistically, Eva1 activates the RelB-dependent noncanonical NF-κB signaling pathway by recruiting TRAF2 to its cytoplasmic tail, thereby promoting GIC proliferation and stemness gene expression.\",\n      \"method\": \"Knockdown and overexpression in GICs, self-renewal/tumor-forming assays, co-immunoprecipitation of TRAF2, NF-κB pathway reporter/western blot analysis\",\n      \"journal\": \"Cancer research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP identifying TRAF2 recruitment plus loss/gain-of-function with defined pathway readout, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"26677976\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"EVA1 (MPZL2) physically interacts with CLCA2 via their transmembrane segments, co-localizes with E-cadherin at cell-cell junctions, and is required for mammary epithelial differentiation; knockdown of EVA1 in immortalized human mammary epithelial cells causes epithelial-to-mesenchymal transition (EMT). EVA1 also participates in a complex with CLCA2 and ZO-1.\",\n      \"method\": \"Membrane dihybrid screening, co-immunoprecipitation, deletion analysis of interacting domains, siRNA knockdown with EMT phenotypic readout, immunofluorescence co-localization\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and deletion mapping of interaction domain, combined with KD phenotype and co-localization, single lab\",\n      \"pmids\": [\"26930581\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Loss-of-function variants in MPZL2 cause autosomal recessive nonsyndromic sensorineural hearing loss. In Mpzl2-mutant mice, there is early-onset progressive sensorineural hearing impairment with histological evidence of altered outer hair cell and supporting cell organization, degeneration of the organ of Corti, and degeneration of spiral ganglion neurons, establishing that MPZL2-mediated cell adhesion is essential for structural integrity of the inner ear epithelium.\",\n      \"method\": \"Homozygosity mapping, whole-exome sequencing, audiometric evaluation of Mpzl2-mutant mice, histological analysis of cochlea\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — human genetics combined with mouse knockout audiometry and cochlear histology, independently replicated across multiple families\",\n      \"pmids\": [\"29961571\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"The MPZL2 protein localizes to auditory inner and outer hair cells in the mouse inner ear with an asymmetric subcellular distribution, as determined by immunolocalization in wild-type mouse cochlear tissue.\",\n      \"method\": \"Immunolocalization/immunofluorescence in mouse inner ear sections\",\n      \"journal\": \"Human genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct subcellular localization experiment in tissue, reported in a second independent study corroborating inner ear expression\",\n      \"pmids\": [\"29982980\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"EVA1A (MPZL2/EVA1) is a lysosome- and endoplasmic reticulum-associated protein that promotes endothelial cell apoptosis and inflammatory activation under proatherogenic disturbed flow. Mechanistically, EVA1A suppresses autophagy under disturbed flow conditions; its knockdown promotes autophagic flux and reduces EC apoptosis. EVA1A expression is transcriptionally regulated by TWIST1 in a flow-direction-dependent manner. In vivo knockdown of the EVA1A orthologue in zebrafish reduced EC apoptosis.\",\n      \"method\": \"siRNA knockdown in human ECs, morpholino knockdown in zebrafish, autophagic flux assay (bafilomycin/LC3-II/p62), flow chamber experiments, zebrafish in vivo validation, ChIP/transcription factor analysis\",\n      \"journal\": \"Arteriosclerosis, thrombosis, and vascular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (in vitro KD, autophagic flux assay, in vivo zebrafish KD), mechanistic pathway placement via TWIST1 and autophagy regulators, replicated across species\",\n      \"pmids\": [\"36794585\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Eva1 (MPZL2) is expressed in macrophages and plays a role in LPS-induced inflammatory responses, possibly through direct interaction with TLR4. Macrophage-specific Eva1 is the key mediator of obesity-induced visceral adipose dysfunction; transplantation of wild-type macrophages into whole-body Eva1 knockout mice abolished the metabolic protection, establishing macrophage-derived Eva1 as the functionally relevant source.\",\n      \"method\": \"Whole-body and adipocyte-specific Eva1 knockout mice, HFD model, macrophage transplantation, co-immunoprecipitation (TLR4 interaction), histological and transcriptomic analysis of adipose tissue\",\n      \"journal\": \"Metabolism: clinical and experimental\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic KO with macrophage reconstitution establishing cell-type specificity, plus Co-IP suggesting TLR4 interaction; single lab\",\n      \"pmids\": [\"40118448\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"AAV-delivered PAM-flexible adenine base editor (ABE8eWQ-SpRY) correcting the homozygous c.220C>T (p.Q74X) mutation in a humanized Mpzl2 mouse model significantly restored hearing function, improved cochlear structural integrity, and reversed altered gene expression, demonstrating that restoration of MPZL2 function is sufficient to rescue the hearing loss phenotype.\",\n      \"method\": \"Humanized knock-in mouse model (hMPZL2Q74X/Q74X), dual-AAV delivery of base editor, ABR audiometry, cochlear histology, RNA-seq\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vivo gene correction with structural, functional, and transcriptomic validation in a humanized model; single lab but multiple orthogonal readouts\",\n      \"pmids\": [\"40764318\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"MPZL2 (EVA1) is an immunoglobulin superfamily adhesion molecule that mediates homophilic cell-cell interactions at epithelial junctions; it is essential for structural integrity of the inner ear organ of Corti (loss causes progressive sensorineural hearing loss in humans and mice), regulates early thymocyte development through epithelial-haematopoietic crosstalk, promotes glioblastoma-initiating cell stemness via TRAF2-dependent noncanonical NF-κB activation, suppresses protective autophagy in endothelial cells under proatherogenic disturbed flow downstream of TWIST1, and mediates macrophage-driven visceral adipose inflammation possibly through TLR4 interaction.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MPZL2 (EVA/EVA1) is an immunoglobulin superfamily transmembrane protein that mediates homophilic cell-cell adhesion and associates with the cytoskeleton, functioning to organize epithelial architecture and tissue integrity [#0]. At epithelial cell-cell junctions it co-localizes with E-cadherin and assembles into a complex with CLCA2 (bound through its transmembrane segment) and ZO-1, and its loss in mammary epithelial cells triggers epithelial-to-mesenchymal transition, marking it as a maintainer of the differentiated epithelial state [#5]. In the inner ear, MPZL2 localizes to auditory hair cells [#7], and loss-of-function variants cause autosomal recessive nonsyndromic sensorineural hearing loss; mutant mice show progressive hearing impairment with disorganization and degeneration of the organ of Corti and spiral ganglion neurons, establishing that MPZL2-mediated adhesion is essential for cochlear structural integrity [#6]. Restoration of MPZL2 function by in vivo base editing of a humanized mutant allele rescues hearing and cochlear structure, demonstrating the phenotype is directly attributable to MPZL2 loss [#10]. Beyond adhesion, MPZL2 has cell-type-specific signaling roles: it is required for early thymocyte development and thymus organization through epithelial-haematopoietic crosstalk [#2, #3], it promotes glioblastoma-initiating cell self-renewal by recruiting TRAF2 to its cytoplasmic tail to activate RelB-dependent noncanonical NF-\\u03baB signaling [#4], it suppresses protective autophagy in endothelial cells under proatherogenic disturbed flow downstream of TWIST1 [#8], and macrophage-derived MPZL2 drives obesity-induced visceral adipose inflammation in conjunction with a TLR4 interaction [#9].\",\n  \"teleology\": [\n    {\n      \"year\": 1998,\n      \"claim\": \"Established MPZL2 as a novel immunoglobulin superfamily molecule capable of homophilic adhesion and cytoskeletal association, framing it as a candidate organizer of thymic epithelial structure.\",\n      \"evidence\": \"RNA fingerprinting, expression analysis in thymic epithelial lines, detergent fractionation, and cell adhesion assay\",\n      \"pmids\": [\n        \"9585423\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model or adhesion-interface mutagenesis\",\n        \"Binding partner mediating adhesion not identified\",\n        \"Cytoskeletal linkage inferred from solubility, not a defined interaction\"\n      ]\n    },\n    {\n      \"year\": 1998,\n      \"claim\": \"Mapped MPZL2 expression to spongiotrophoblast and invasive glycogen cells during placentation, raising the possibility of a role in trophoblast invasion.\",\n      \"evidence\": \"In situ hybridization across mouse placental development\",\n      \"pmids\": [\n        \"9883583\"\n      ],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Expression only; no loss-of-function test of placental function\",\n        \"No mechanistic link to adhesion activity established\"\n      ]\n    },\n    {\n      \"year\": 2007,\n      \"claim\": \"Showed that gain of MPZL2 in the thymic cortex enlarges the stromal compartment and increases thymocyte numbers, supporting a structural-organizational role in thymus development.\",\n      \"evidence\": \"Transgenic mouse overexpression with histology and flow cytometry\",\n      \"pmids\": [\n        \"17362876\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Gain-of-function only; does not define the requirement\",\n        \"Molecular mechanism linking adhesion to stromal expansion unresolved\"\n      ]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Demonstrated a cell-autonomous requirement for MPZL2 in early T lymphocyte development, advancing from correlation to functional necessity.\",\n      \"evidence\": \"RNAi knockdown in hematopoietic progenitors, OP9-DL1 co-culture, and Rag2-\\u03b3c DKO reconstitution with flow cytometry\",\n      \"pmids\": [\n        \"19851463\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Signaling pathway downstream of MPZL2 in thymocytes not defined\",\n        \"Adhesion partner driving the DN1-DN3 transition unknown\"\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Identified a signaling output for MPZL2 by showing it recruits TRAF2 to its cytoplasmic tail to drive noncanonical NF-\\u03baB activation supporting glioblastoma stem cell self-renewal, extending its role beyond passive adhesion.\",\n      \"evidence\": \"Knockdown/overexpression in glioblastoma-initiating cells, TRAF2 co-immunoprecipitation, NF-\\u03baB reporter and western blot\",\n      \"pmids\": [\n        \"26677976\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Cytoplasmic motif mediating TRAF2 binding not mapped\",\n        \"Whether this pathway operates in normal epithelia untested\",\n        \"Upstream ligand/adhesion event triggering signaling unknown\"\n      ]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Placed MPZL2 in a defined junctional complex with CLCA2 and ZO-1 alongside E-cadherin and showed its loss drives EMT, mechanistically tying it to maintenance of the epithelial state.\",\n      \"evidence\": \"Membrane dihybrid screen, reciprocal co-IP with transmembrane deletion mapping, siRNA with EMT readout, immunofluorescence co-localization\",\n      \"pmids\": [\n        \"26930581\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional consequence of CLCA2 binding for adhesion not dissected\",\n        \"Connection between junctional complex and EMT signaling unresolved\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Established MPZL2 as a Mendelian deafness gene and showed its adhesion function is essential for cochlear structural integrity, with hair-cell localization supporting the site of action.\",\n      \"evidence\": \"Homozygosity mapping and exome sequencing in families, Mpzl2-mutant mouse audiometry and cochlear histology, plus immunolocalization to inner ear hair cells\",\n      \"pmids\": [\n        \"29961571\",\n        \"29982980\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Adhesion partner in the organ of Corti not identified\",\n        \"Why degeneration is progressive rather than developmental unclear\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Revealed a non-adhesion, organelle-associated role in which MPZL2 suppresses protective autophagy and promotes endothelial apoptosis under disturbed flow, placing it downstream of TWIST1 in a flow-dependent atherogenic circuit.\",\n      \"evidence\": \"siRNA in human ECs, autophagic flux assays, flow chamber, ChIP/TF analysis, and zebrafish morpholino knockdown\",\n      \"pmids\": [\n        \"36794585\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Molecular mechanism by which MPZL2 inhibits autophagy not defined\",\n        \"Relationship between adhesion role and autophagy suppression unresolved\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Defined macrophage-derived MPZL2 as the functionally relevant driver of obesity-induced visceral adipose inflammation, with a TLR4 interaction as candidate mechanism.\",\n      \"evidence\": \"Whole-body and adipocyte-specific knockout mice, HFD model, macrophage transplantation rescue, and TLR4 co-immunoprecipitation\",\n      \"pmids\": [\n        \"40118448\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"TLR4 interaction shown by Co-IP only, not reciprocally validated functionally\",\n        \"Whether MPZL2 modulates TLR4 signaling output directly untested\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Demonstrated that restoring MPZL2 function is sufficient to reverse hearing loss, confirming the gene's causal role and establishing therapeutic tractability.\",\n      \"evidence\": \"Dual-AAV adenine base editor correction of c.220C>T in a humanized Mpzl2 knock-in mouse with ABR audiometry, cochlear histology, and RNA-seq\",\n      \"pmids\": [\n        \"40764318\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Durability and developmental timing window of rescue not fully defined\",\n        \"Does not resolve the molecular adhesion mechanism in the cochlea\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The unifying biochemical mechanism connecting MPZL2's homophilic adhesion to its diverse signaling outputs (TRAF2/NF-\\u03baB, autophagy suppression, TLR4) remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structure of the adhesion interface or cytoplasmic signaling motifs\",\n        \"The physiological homophilic/heterophilic ligand in each tissue is undefined\",\n        \"Whether adhesion and signaling roles are separable functions is untested\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\n        \"term_id\": \"GO:0098631\",\n        \"supporting_discovery_ids\": [\n          0,\n          5,\n          6\n        ]\n      },\n      {\n        \"term_id\": \"GO:0060089\",\n        \"supporting_discovery_ids\": [\n          4\n        ]\n      }\n    ],\n    \"localization\": [\n      {\n        \"term_id\": \"GO:0005886\",\n        \"supporting_discovery_ids\": [\n          0,\n          5,\n          7\n        ]\n      },\n      {\n        \"term_id\": \"GO:0005764\",\n        \"supporting_discovery_ids\": [\n          8\n        ]\n      },\n      {\n        \"term_id\": \"GO:0005783\",\n        \"supporting_discovery_ids\": [\n          8\n        ]\n      }\n    ],\n    \"pathway\": [\n      {\n        \"term_id\": \"R-HSA-162582\",\n        \"supporting_discovery_ids\": [\n          4\n        ]\n      },\n      {\n        \"term_id\": \"R-HSA-9612973\",\n        \"supporting_discovery_ids\": [\n          8\n        ]\n      },\n      {\n        \"term_id\": \"R-HSA-1266738\",\n        \"supporting_discovery_ids\": [\n          2,\n          3,\n          6\n        ]\n      }\n    ],\n    \"complexes\": [\n      \"CLCA2-ZO-1 junctional complex\"\n    ],\n    \"partners\": [\n      \"CLCA2\",\n      \"ZO-1\",\n      \"TRAF2\",\n      \"TLR4\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":5,"faith_total":5,"faith_pct":100.0}}