{"gene":"MSN","run_date":"2026-06-10T02:59:51","timeline":{"discoveries":[{"year":2001,"finding":"MSN (moesin) was identified as a fusion partner for ALK in anaplastic large cell lymphoma. The hybrid MSN-ALK protein (125 kDa) contains an active tyrosine kinase domain, and the unique membrane-restricted ALK staining pattern reflects association of moesin with cell membrane proteins. The ALK breakpoint occurred within exonic sequence coding for the juxtamembrane portion of ALK, and genomic breakpoint analysis confirmed in-frame fusion of MSN intron 10 to a shorter juxtamembrane exon of ALK.","method":"Molecular cloning, immunohistochemistry, genomic breakpoint sequencing, Western blot","journal":"Laboratory investigation; a journal of technical methods and pathology","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal molecular characterization with multiple orthogonal methods (IHC, Western blot, genomic sequencing), replicated by a second independent case report (PMID:15297972)","pmids":["11310834","15297972"],"is_preprint":false},{"year":2016,"finding":"Hemizygous loss-of-function mutations in MSN (including R171W missense in the FERM domain and R533X nonsense) cause X-linked primary immunodeficiency characterized by profound lymphopenia, hypogammaglobulinemia, poor T-cell proliferation, reduced naive T cells, elevated CD57+ senescent CD8+ T cells, poor chemokine receptor expression, increased adhesion molecule expression, and altered migration and adhesion. T-cell proliferation defects were rescued by re-expression of wild-type MSN, establishing direct causality.","method":"Genetic analysis (exome/targeted sequencing), flow cytometry, T-cell proliferation assays, wild-type MSN rescue experiment, migration/adhesion assays","journal":"The Journal of allergy and clinical immunology","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods including functional rescue with wild-type MSN, 7 patients from 5 families, two distinct mutation types characterized","pmids":["27405666"],"is_preprint":false},{"year":2020,"finding":"MSN physically interacts with the nuclear protein NONO. Phosphorylated MSN undergoes NONO-assisted nuclear localization via protein kinase C (PKC). Once in the nucleus, PKC-bound MSN activates CREB signaling through PKC-mediated phosphorylation of CREB. This pathway promotes breast cancer cell proliferation and invasion in vitro and tumor growth in vivo.","method":"Co-immunoprecipitation, nuclear fractionation/localization assays, phosphorylation assays, shRNA knockdown, in vitro proliferation/invasion assays, in vivo xenograft","journal":"Science advances","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — co-IP and nuclear fractionation with functional validation in vitro and in vivo, single lab with multiple orthogonal methods","pmids":["32128390"],"is_preprint":false},{"year":2018,"finding":"Loss of XIST lncRNA activates c-Met signaling via MSN-mediated protein stabilization, promoting stemness and epithelial-mesenchymal transition in breast cancer cells. MSN was shown to stabilize c-Met protein, and this MSN-c-Met axis contributes to brain metastasis.","method":"XIST silencing/knockout, Western blot for c-Met protein levels, xenograft and GEMM models, gene expression analysis","journal":"Cancer research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional knockdown with in vivo validation in xenograft and GEMM models, single lab","pmids":["30026327"],"is_preprint":false},{"year":1994,"finding":"The MSN gene encoding moesin was mapped to Xq11.2-q12. The gene spans >30 kb with 12 exons; exon/intron junctions demarcate individual highly conserved protein domains. Primer extension analysis identified two major transcription start sites. The 5'-flanking region is GC-rich, lacks a TATA box, and contains SP1 and AP1 binding sites.","method":"Southern blot, Western blot, somatic cell hybrid analysis, fluorescence in situ hybridization (FISH), primer extension, genomic sequencing","journal":"Genomics","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal mapping methods, gene structure determined by direct genomic sequencing and functional promoter element identification","pmids":["8188263"],"is_preprint":false},{"year":2023,"finding":"The FERM domain of MSN directly interacts with the cytoplasmic tail of CD44. Structural, mutational, and phage-display studies revealed an allosteric site near the PIP2 binding pocket of the FERM domain that influences CD44 binding. PIP2 binding to the FERM domain stimulates CD44 binding through an allosteric mechanism, creating a neighboring pocket for receptor tail accommodation. Small molecule inhibitors of the MSN-CD44 interaction were identified by high-throughput screening.","method":"Structural studies (crystal/biophysical), site-directed mutagenesis, phage display, high-throughput chemical library screening, binding assays","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — structural, mutational, and phage-display studies in a single rigorous study with multiple orthogonal methods identifying allosteric mechanism","pmids":["37866628"],"is_preprint":false},{"year":2025,"finding":"MSN activates the PI3K/mTOR signaling pathway in glioma stem cells (GSCs), driving proneural-to-mesenchymal transition (PMT). This enhances repair of DNA damage caused by radiotherapy and temozolomide, increasing chemoradiotherapy resistance. GNE-317, a small molecule inhibitor, specifically inhibits MSN and suppresses downstream PI3K/mTOR activation, reversing PMT and sensitizing GSCs to chemoradiotherapy.","method":"MSN knockdown/overexpression, Western blot for PI3K/mTOR pathway components, in vitro and in vivo chemoradiotherapy resistance assays, small molecule inhibitor treatment","journal":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional KD/OE with defined pathway readout (PI3K/mTOR) and in vivo validation, single lab","pmids":["39921260"],"is_preprint":false},{"year":2020,"finding":"MSN silencing significantly decreased invasiveness of bladder urothelial carcinoma cell lines in a 3D invasion assay, establishing a functional role for MSN in cancer cell invasion.","method":"shRNA knockdown, 3D in vitro invasion assay, proteomics","journal":"Cancers","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single functional method (3D invasion), no pathway placement","pmids":["32326232"],"is_preprint":false},{"year":2023,"finding":"MSN promotes colorectal cancer progression via the β-catenin–RUNX2 signaling axis. MSN silencing decreased cytoplasmic and nuclear β-catenin levels; pharmacological inhibition of β-catenin in MSN-overexpressing cells reduced RUNX2 expression; activating β-catenin by inhibiting GSK3β rescued RUNX2 downregulation in MSN-knockdown cells, confirming MSN regulates RUNX2 via β-catenin.","method":"shRNA knockdown, plasmid overexpression, Western blot, RNA sequencing, pharmacological β-catenin/GSK3β modulation, cell proliferation/migration assays","journal":"International journal of molecular sciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis via pharmacological rescue experiments placing MSN upstream of β-catenin–RUNX2 axis, multiple orthogonal methods, single lab","pmids":["37446127"],"is_preprint":false},{"year":2022,"finding":"MSN stabilizes PD-L1 protein in hepatocellular carcinoma cells. miR-133a-3p targets MSN (validated by dual-luciferase reporter assay), and MSN inhibits the antitumor effect of APS by maintaining PD-L1 stability.","method":"Western blot for PD-L1 protein levels, dual-luciferase reporter assay for miR-133a-3p/MSN interaction, flow cytometry, shRNA knockdown","journal":"Pharmaceutical biology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, limited mechanistic follow-up on how MSN stabilizes PD-L1; luciferase confirms miRNA-MSN interaction only","pmids":["36086826"],"is_preprint":false},{"year":2022,"finding":"Hemizygous nonsense mutation W217X in MSN results in significantly decreased MSN mRNA expression and causes an autoimmune phenotype (antiphospholipid syndrome, Hashimoto's thyroiditis, leg ulcers, juvenile tooth loss) with immune dysregulation including low naive T cells and elevated activated T-helper cells, extending the known phenotypic spectrum of MSN loss-of-function.","method":"Whole exome sequencing, flow cytometry immunophenotyping, qRT-PCR for MSN mRNA expression","journal":"Frontiers in immunology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — genetic and immunophenotyping data only, no functional rescue; extends clinical spectrum rather than establishing new mechanism","pmids":["36119109"],"is_preprint":false}],"current_model":"MSN (moesin) is an ERM-family protein whose FERM domain binds phosphatidylinositol 4,5-bisphosphate (PIP2) and the cytoplasmic tail of CD44 via an allosteric mechanism, linking the plasma membrane to the actin cytoskeleton; loss-of-function mutations (R171W, R533X, W217X) in the FERM domain cause X-linked primary immunodeficiency with defective T-cell proliferation, migration, and adhesion; in cancer contexts, MSN can form an oncogenic MSN-ALK fusion kinase localized to the plasma membrane, undergoes PKC-mediated phosphorylation and NONO-assisted nuclear translocation to activate CREB signaling, stabilizes c-Met protein, activates PI3K/mTOR to drive proneural-to-mesenchymal transition and chemoradiotherapy resistance, and promotes colorectal cancer progression via the β-catenin–RUNX2 axis."},"narrative":{"mechanistic_narrative":"MSN (moesin) is an ERM-family membrane-cytoskeleton linker whose FERM domain directly binds the cytoplasmic tail of the receptor CD44, with PIP2 binding to the FERM domain allosterically stimulating CD44 engagement through a neighboring receptor-tail pocket [PMID:37866628]. Hemizygous loss-of-function mutations in the MSN FERM domain (R171W missense, R533X nonsense) cause X-linked primary immunodeficiency marked by lymphopenia, poor T-cell proliferation, and altered migration and adhesion, with the proliferation defect rescued by wild-type MSN re-expression [PMID:27405666]. In oncogenic contexts MSN serves both as a structural fusion partner and as a signaling node: it fuses to ALK to generate a membrane-localized 125 kDa MSN-ALK tyrosine kinase in anaplastic large cell lymphoma [PMID:11310834, PMID:15297972], and as full-length protein it drives tumor progression through multiple pathways—PKC-dependent phosphorylation and NONO-assisted nuclear translocation to activate CREB [PMID:32128390], stabilization of c-Met protein [PMID:30026327], activation of PI3K/mTOR to drive proneural-to-mesenchymal transition and chemoradiotherapy resistance in glioma stem cells [PMID:39921260], and promotion of colorectal cancer via the β-catenin–RUNX2 axis [PMID:37446127].","teleology":[{"year":1994,"claim":"Establishing the genomic organization and chromosomal location of MSN provided the structural foundation by demarcating its conserved protein domains and X-linked locus.","evidence":"Somatic cell hybrid analysis, FISH, primer extension, and genomic sequencing","pmids":["8188263"],"confidence":"High","gaps":["Does not establish protein function","Promoter element activity (SP1/AP1) not functionally tested in vivo"]},{"year":2001,"claim":"Identification of MSN as an ALK fusion partner showed that MSN's membrane-association capacity can be coopted to mislocalize and activate a tyrosine kinase, defining a structural-oncogenic role.","evidence":"Molecular cloning, IHC, genomic breakpoint sequencing, and Western blot in anaplastic large cell lymphoma","pmids":["11310834","15297972"],"confidence":"High","gaps":["Downstream signaling of MSN-ALK not mechanistically dissected here","Contribution of the MSN portion to kinase activity vs. localization not separated"]},{"year":2016,"claim":"Loss-of-function genetics established MSN as causally required for normal T-cell proliferation, migration, and adhesion, defining its physiological role in immunity.","evidence":"Exome/targeted sequencing, flow cytometry, proliferation assays, and wild-type MSN rescue across 7 patients from 5 families","pmids":["27405666"],"confidence":"High","gaps":["Molecular link between FERM mutations and migration/adhesion defects not resolved","Whether defects are cell-intrinsic to T cells only is not fully defined"]},{"year":2018,"claim":"Demonstrating MSN-mediated c-Met protein stabilization placed MSN within a regulatory circuit controlling stemness and EMT in breast cancer.","evidence":"XIST silencing/knockout, Western blot for c-Met, and xenograft/GEMM models","pmids":["30026327"],"confidence":"Medium","gaps":["Mechanism by which MSN stabilizes c-Met not defined","Single lab; direct MSN–c-Met physical interaction not shown"]},{"year":2020,"claim":"Discovery of phosphorylated MSN nuclear translocation via NONO and PKC redefined MSN as a signaling effector that activates CREB beyond its membrane role.","evidence":"Co-IP, nuclear fractionation, phosphorylation assays, shRNA, and in vitro/in vivo breast cancer models","pmids":["32128390"],"confidence":"Medium","gaps":["Reciprocal validation of MSN-NONO interaction limited","Phosphosite(s) driving nuclear import not mapped"]},{"year":2023,"claim":"Structural and biophysical dissection of the FERM domain revealed an allosteric mechanism by which PIP2 binding stimulates CD44 tail engagement, mechanistically defining MSN's membrane-receptor linkage.","evidence":"Structural studies, site-directed mutagenesis, phage display, and HTS for small-molecule inhibitors","pmids":["37866628"],"confidence":"High","gaps":["Cellular consequences of disrupting the allosteric site not tested","Connection to disease mutations (R171W) not directly examined"]},{"year":2023,"claim":"Epistasis experiments placed MSN upstream of a β-catenin–RUNX2 axis, defining a transcriptional output of MSN signaling in colorectal cancer.","evidence":"shRNA, overexpression, RNA-seq, and pharmacological β-catenin/GSK3β rescue in colorectal cancer cells","pmids":["37446127"],"confidence":"Medium","gaps":["Direct molecular link between MSN and β-catenin stabilization not defined","Single lab"]},{"year":2025,"claim":"Linking MSN to PI3K/mTOR-driven proneural-to-mesenchymal transition connected MSN to therapy resistance and provided a druggable axis in glioma stem cells.","evidence":"MSN KD/OE, Western blot for PI3K/mTOR components, chemoradiotherapy resistance assays, and GNE-317 inhibitor treatment in vitro and in vivo","pmids":["39921260"],"confidence":"Medium","gaps":["How MSN activates PI3K/mTOR mechanistically not resolved","GNE-317 specificity for MSN not fully established"]},{"year":null,"claim":"How MSN's defined membrane-cytoskeleton linker activity (FERM/PIP2/CD44) mechanistically connects to its diverse downstream oncogenic signaling outputs (c-Met, CREB, β-catenin, PI3K/mTOR) and to the T-cell defects of immunodeficiency remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unified mechanism linking membrane scaffolding to nuclear/signaling roles","Substrate or direct binding events for most oncogenic axes undefined","Structure-function link between disease mutations and specific molecular activities not established"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[5]},{"term_id":"GO:0008289","term_label":"lipid binding","supporting_discovery_ids":[5]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[5]}],"localization":[{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[0,5]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[2,6,8]},{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[1]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[0]}],"complexes":[],"partners":["CD44","ALK","NONO"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P26038","full_name":"Moesin","aliases":["Membrane-organizing extension spike protein"],"length_aa":577,"mass_kda":67.8,"function":"Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Also participates in immunologic synapse formation (PubMed:27405666)","subcellular_location":"Cell membrane; Cytoplasm, cytoskeleton; Apical cell membrane; Cell projection, microvillus membrane; Cell projection, microvillus","url":"https://www.uniprot.org/uniprotkb/P26038/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/MSN","classification":"Not Classified","n_dependent_lines":29,"n_total_lines":1208,"dependency_fraction":0.024006622516556293},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000147065","cell_line_id":"CID000886","localizations":[{"compartment":"cytoplasmic","grade":3},{"compartment":"nucleoplasm","grade":1}],"interactors":[{"gene":"EZR","stoichiometry":4.0},{"gene":"CD151","stoichiometry":0.2},{"gene":"KIAA0319L","stoichiometry":0.2},{"gene":"LAMP2","stoichiometry":0.2},{"gene":"PFDN1","stoichiometry":0.2},{"gene":"RDX","stoichiometry":0.2},{"gene":"KIAA1033","stoichiometry":0.2},{"gene":"AATF","stoichiometry":0.2},{"gene":"MNS1","stoichiometry":0.2},{"gene":"CNTRL","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID000886","total_profiled":1310},"omim":[{"mim_id":"621003","title":"TRANSCRIPTION FACTOR Sp9; SP9","url":"https://www.omim.org/entry/621003"},{"mim_id":"617467","title":"FERM DOMAIN-CONTAINING PROTEIN 4B; FRMD4B","url":"https://www.omim.org/entry/617467"},{"mim_id":"614555","title":"FERM DOMAIN-CONTAINING PROTEIN 6; FRMD6","url":"https://www.omim.org/entry/614555"},{"mim_id":"614235","title":"PDZ DOMAIN-CONTAINING PROTEIN 8; PDZD8","url":"https://www.omim.org/entry/614235"},{"mim_id":"613351","title":"RHO GTPase-ACTIVATING PROTEIN 18; ARHGAP18","url":"https://www.omim.org/entry/613351"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Plasma membrane","reliability":"Enhanced"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/MSN"},"hgnc":{"alias_symbol":[],"prev_symbol":[]},"alphafold":{"accession":"P26038","domains":[{"cath_id":"3.10.20.90","chopping":"4-81","consensus_level":"high","plddt":94.8336,"start":4,"end":81}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P26038","model_url":"https://alphafold.ebi.ac.uk/files/AF-P26038-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P26038-F1-predicted_aligned_error_v6.png","plddt_mean":86.38},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=MSN","jax_strain_url":"https://www.jax.org/strain/search?query=MSN"},"sequence":{"accession":"P26038","fasta_url":"https://rest.uniprot.org/uniprotkb/P26038.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P26038/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P26038"}},"corpus_meta":[{"pmid":"24142549","id":"PMC_24142549","title":"MSN anti-cancer nanomedicines: chemotherapy enhancement, overcoming of drug resistance, and metastasis inhibition.","date":"2013","source":"Advanced materials (Deerfield Beach, Fla.)","url":"https://pubmed.ncbi.nlm.nih.gov/24142549","citation_count":316,"is_preprint":false},{"pmid":"30026327","id":"PMC_30026327","title":"Loss of XIST in Breast Cancer Activates MSN-c-Met and Reprograms Microglia via Exosomal miRNA to Promote Brain Metastasis.","date":"2018","source":"Cancer research","url":"https://pubmed.ncbi.nlm.nih.gov/30026327","citation_count":262,"is_preprint":false},{"pmid":"25159109","id":"PMC_25159109","title":"MSN-mediated sequential vascular-to-cell nuclear-targeted drug delivery for efficient tumor regression.","date":"2014","source":"Advanced materials (Deerfield Beach, Fla.)","url":"https://pubmed.ncbi.nlm.nih.gov/25159109","citation_count":185,"is_preprint":false},{"pmid":"21533799","id":"PMC_21533799","title":"Drugs of abuse screening in urine as part of a metabolite-based LC-MSn screening concept.","date":"2011","source":"Analytical and bioanalytical chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/21533799","citation_count":118,"is_preprint":false},{"pmid":"12645918","id":"PMC_12645918","title":"Targeted proteomics of low-level proteins in human plasma by LC/MSn: using human growth hormone as a model system.","date":"2002","source":"Journal of proteome research","url":"https://pubmed.ncbi.nlm.nih.gov/12645918","citation_count":106,"is_preprint":false},{"pmid":"11310834","id":"PMC_11310834","title":"Molecular characterization of a new ALK translocation involving moesin (MSN-ALK) in anaplastic large cell lymphoma.","date":"2001","source":"Laboratory investigation; 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The hybrid MSN-ALK protein (125 kDa) contains an active tyrosine kinase domain, and the unique membrane-restricted ALK staining pattern reflects association of moesin with cell membrane proteins. The ALK breakpoint occurred within exonic sequence coding for the juxtamembrane portion of ALK, and genomic breakpoint analysis confirmed in-frame fusion of MSN intron 10 to a shorter juxtamembrane exon of ALK.\",\n      \"method\": \"Molecular cloning, immunohistochemistry, genomic breakpoint sequencing, Western blot\",\n      \"journal\": \"Laboratory investigation; a journal of technical methods and pathology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal molecular characterization with multiple orthogonal methods (IHC, Western blot, genomic sequencing), replicated by a second independent case report (PMID:15297972)\",\n      \"pmids\": [\"11310834\", \"15297972\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Hemizygous loss-of-function mutations in MSN (including R171W missense in the FERM domain and R533X nonsense) cause X-linked primary immunodeficiency characterized by profound lymphopenia, hypogammaglobulinemia, poor T-cell proliferation, reduced naive T cells, elevated CD57+ senescent CD8+ T cells, poor chemokine receptor expression, increased adhesion molecule expression, and altered migration and adhesion. T-cell proliferation defects were rescued by re-expression of wild-type MSN, establishing direct causality.\",\n      \"method\": \"Genetic analysis (exome/targeted sequencing), flow cytometry, T-cell proliferation assays, wild-type MSN rescue experiment, migration/adhesion assays\",\n      \"journal\": \"The Journal of allergy and clinical immunology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods including functional rescue with wild-type MSN, 7 patients from 5 families, two distinct mutation types characterized\",\n      \"pmids\": [\"27405666\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"MSN physically interacts with the nuclear protein NONO. Phosphorylated MSN undergoes NONO-assisted nuclear localization via protein kinase C (PKC). Once in the nucleus, PKC-bound MSN activates CREB signaling through PKC-mediated phosphorylation of CREB. This pathway promotes breast cancer cell proliferation and invasion in vitro and tumor growth in vivo.\",\n      \"method\": \"Co-immunoprecipitation, nuclear fractionation/localization assays, phosphorylation assays, shRNA knockdown, in vitro proliferation/invasion assays, in vivo xenograft\",\n      \"journal\": \"Science advances\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — co-IP and nuclear fractionation with functional validation in vitro and in vivo, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"32128390\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Loss of XIST lncRNA activates c-Met signaling via MSN-mediated protein stabilization, promoting stemness and epithelial-mesenchymal transition in breast cancer cells. MSN was shown to stabilize c-Met protein, and this MSN-c-Met axis contributes to brain metastasis.\",\n      \"method\": \"XIST silencing/knockout, Western blot for c-Met protein levels, xenograft and GEMM models, gene expression analysis\",\n      \"journal\": \"Cancer research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional knockdown with in vivo validation in xenograft and GEMM models, single lab\",\n      \"pmids\": [\"30026327\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1994,\n      \"finding\": \"The MSN gene encoding moesin was mapped to Xq11.2-q12. The gene spans >30 kb with 12 exons; exon/intron junctions demarcate individual highly conserved protein domains. Primer extension analysis identified two major transcription start sites. The 5'-flanking region is GC-rich, lacks a TATA box, and contains SP1 and AP1 binding sites.\",\n      \"method\": \"Southern blot, Western blot, somatic cell hybrid analysis, fluorescence in situ hybridization (FISH), primer extension, genomic sequencing\",\n      \"journal\": \"Genomics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal mapping methods, gene structure determined by direct genomic sequencing and functional promoter element identification\",\n      \"pmids\": [\"8188263\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"The FERM domain of MSN directly interacts with the cytoplasmic tail of CD44. Structural, mutational, and phage-display studies revealed an allosteric site near the PIP2 binding pocket of the FERM domain that influences CD44 binding. PIP2 binding to the FERM domain stimulates CD44 binding through an allosteric mechanism, creating a neighboring pocket for receptor tail accommodation. Small molecule inhibitors of the MSN-CD44 interaction were identified by high-throughput screening.\",\n      \"method\": \"Structural studies (crystal/biophysical), site-directed mutagenesis, phage display, high-throughput chemical library screening, binding assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — structural, mutational, and phage-display studies in a single rigorous study with multiple orthogonal methods identifying allosteric mechanism\",\n      \"pmids\": [\"37866628\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"MSN activates the PI3K/mTOR signaling pathway in glioma stem cells (GSCs), driving proneural-to-mesenchymal transition (PMT). This enhances repair of DNA damage caused by radiotherapy and temozolomide, increasing chemoradiotherapy resistance. GNE-317, a small molecule inhibitor, specifically inhibits MSN and suppresses downstream PI3K/mTOR activation, reversing PMT and sensitizing GSCs to chemoradiotherapy.\",\n      \"method\": \"MSN knockdown/overexpression, Western blot for PI3K/mTOR pathway components, in vitro and in vivo chemoradiotherapy resistance assays, small molecule inhibitor treatment\",\n      \"journal\": \"Advanced science (Weinheim, Baden-Wurttemberg, Germany)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional KD/OE with defined pathway readout (PI3K/mTOR) and in vivo validation, single lab\",\n      \"pmids\": [\"39921260\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"MSN silencing significantly decreased invasiveness of bladder urothelial carcinoma cell lines in a 3D invasion assay, establishing a functional role for MSN in cancer cell invasion.\",\n      \"method\": \"shRNA knockdown, 3D in vitro invasion assay, proteomics\",\n      \"journal\": \"Cancers\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single functional method (3D invasion), no pathway placement\",\n      \"pmids\": [\"32326232\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"MSN promotes colorectal cancer progression via the β-catenin–RUNX2 signaling axis. MSN silencing decreased cytoplasmic and nuclear β-catenin levels; pharmacological inhibition of β-catenin in MSN-overexpressing cells reduced RUNX2 expression; activating β-catenin by inhibiting GSK3β rescued RUNX2 downregulation in MSN-knockdown cells, confirming MSN regulates RUNX2 via β-catenin.\",\n      \"method\": \"shRNA knockdown, plasmid overexpression, Western blot, RNA sequencing, pharmacological β-catenin/GSK3β modulation, cell proliferation/migration assays\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis via pharmacological rescue experiments placing MSN upstream of β-catenin–RUNX2 axis, multiple orthogonal methods, single lab\",\n      \"pmids\": [\"37446127\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"MSN stabilizes PD-L1 protein in hepatocellular carcinoma cells. miR-133a-3p targets MSN (validated by dual-luciferase reporter assay), and MSN inhibits the antitumor effect of APS by maintaining PD-L1 stability.\",\n      \"method\": \"Western blot for PD-L1 protein levels, dual-luciferase reporter assay for miR-133a-3p/MSN interaction, flow cytometry, shRNA knockdown\",\n      \"journal\": \"Pharmaceutical biology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, limited mechanistic follow-up on how MSN stabilizes PD-L1; luciferase confirms miRNA-MSN interaction only\",\n      \"pmids\": [\"36086826\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Hemizygous nonsense mutation W217X in MSN results in significantly decreased MSN mRNA expression and causes an autoimmune phenotype (antiphospholipid syndrome, Hashimoto's thyroiditis, leg ulcers, juvenile tooth loss) with immune dysregulation including low naive T cells and elevated activated T-helper cells, extending the known phenotypic spectrum of MSN loss-of-function.\",\n      \"method\": \"Whole exome sequencing, flow cytometry immunophenotyping, qRT-PCR for MSN mRNA expression\",\n      \"journal\": \"Frontiers in immunology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — genetic and immunophenotyping data only, no functional rescue; extends clinical spectrum rather than establishing new mechanism\",\n      \"pmids\": [\"36119109\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"MSN (moesin) is an ERM-family protein whose FERM domain binds phosphatidylinositol 4,5-bisphosphate (PIP2) and the cytoplasmic tail of CD44 via an allosteric mechanism, linking the plasma membrane to the actin cytoskeleton; loss-of-function mutations (R171W, R533X, W217X) in the FERM domain cause X-linked primary immunodeficiency with defective T-cell proliferation, migration, and adhesion; in cancer contexts, MSN can form an oncogenic MSN-ALK fusion kinase localized to the plasma membrane, undergoes PKC-mediated phosphorylation and NONO-assisted nuclear translocation to activate CREB signaling, stabilizes c-Met protein, activates PI3K/mTOR to drive proneural-to-mesenchymal transition and chemoradiotherapy resistance, and promotes colorectal cancer progression via the β-catenin–RUNX2 axis.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MSN (moesin) is an ERM-family membrane-cytoskeleton linker whose FERM domain directly binds the cytoplasmic tail of the receptor CD44, with PIP2 binding to the FERM domain allosterically stimulating CD44 engagement through a neighboring receptor-tail pocket [#5]. Hemizygous loss-of-function mutations in the MSN FERM domain (R171W missense, R533X nonsense) cause X-linked primary immunodeficiency marked by lymphopenia, poor T-cell proliferation, and altered migration and adhesion, with the proliferation defect rescued by wild-type MSN re-expression [#1]. In oncogenic contexts MSN serves both as a structural fusion partner and as a signaling node: it fuses to ALK to generate a membrane-localized 125 kDa MSN-ALK tyrosine kinase in anaplastic large cell lymphoma [#0], and as full-length protein it drives tumor progression through multiple pathways—PKC-dependent phosphorylation and NONO-assisted nuclear translocation to activate CREB [#2], stabilization of c-Met protein [#3], activation of PI3K/mTOR to drive proneural-to-mesenchymal transition and chemoradiotherapy resistance in glioma stem cells [#6], and promotion of colorectal cancer via the \\u03b2-catenin\\u2013RUNX2 axis [#8].\",\n  \"teleology\": [\n    {\n      \"year\": 1994,\n      \"claim\": \"Establishing the genomic organization and chromosomal location of MSN provided the structural foundation by demarcating its conserved protein domains and X-linked locus.\",\n      \"evidence\": \"Somatic cell hybrid analysis, FISH, primer extension, and genomic sequencing\",\n      \"pmids\": [\"8188263\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not establish protein function\", \"Promoter element activity (SP1/AP1) not functionally tested in vivo\"]\n    },\n    {\n      \"year\": 2001,\n      \"claim\": \"Identification of MSN as an ALK fusion partner showed that MSN's membrane-association capacity can be coopted to mislocalize and activate a tyrosine kinase, defining a structural-oncogenic role.\",\n      \"evidence\": \"Molecular cloning, IHC, genomic breakpoint sequencing, and Western blot in anaplastic large cell lymphoma\",\n      \"pmids\": [\"11310834\", \"15297972\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Downstream signaling of MSN-ALK not mechanistically dissected here\", \"Contribution of the MSN portion to kinase activity vs. localization not separated\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Loss-of-function genetics established MSN as causally required for normal T-cell proliferation, migration, and adhesion, defining its physiological role in immunity.\",\n      \"evidence\": \"Exome/targeted sequencing, flow cytometry, proliferation assays, and wild-type MSN rescue across 7 patients from 5 families\",\n      \"pmids\": [\"27405666\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular link between FERM mutations and migration/adhesion defects not resolved\", \"Whether defects are cell-intrinsic to T cells only is not fully defined\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Demonstrating MSN-mediated c-Met protein stabilization placed MSN within a regulatory circuit controlling stemness and EMT in breast cancer.\",\n      \"evidence\": \"XIST silencing/knockout, Western blot for c-Met, and xenograft/GEMM models\",\n      \"pmids\": [\"30026327\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism by which MSN stabilizes c-Met not defined\", \"Single lab; direct MSN\\u2013c-Met physical interaction not shown\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Discovery of phosphorylated MSN nuclear translocation via NONO and PKC redefined MSN as a signaling effector that activates CREB beyond its membrane role.\",\n      \"evidence\": \"Co-IP, nuclear fractionation, phosphorylation assays, shRNA, and in vitro/in vivo breast cancer models\",\n      \"pmids\": [\"32128390\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Reciprocal validation of MSN-NONO interaction limited\", \"Phosphosite(s) driving nuclear import not mapped\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Structural and biophysical dissection of the FERM domain revealed an allosteric mechanism by which PIP2 binding stimulates CD44 tail engagement, mechanistically defining MSN's membrane-receptor linkage.\",\n      \"evidence\": \"Structural studies, site-directed mutagenesis, phage display, and HTS for small-molecule inhibitors\",\n      \"pmids\": [\"37866628\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Cellular consequences of disrupting the allosteric site not tested\", \"Connection to disease mutations (R171W) not directly examined\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Epistasis experiments placed MSN upstream of a \\u03b2-catenin\\u2013RUNX2 axis, defining a transcriptional output of MSN signaling in colorectal cancer.\",\n      \"evidence\": \"shRNA, overexpression, RNA-seq, and pharmacological \\u03b2-catenin/GSK3\\u03b2 rescue in colorectal cancer cells\",\n      \"pmids\": [\"37446127\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct molecular link between MSN and \\u03b2-catenin stabilization not defined\", \"Single lab\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Linking MSN to PI3K/mTOR-driven proneural-to-mesenchymal transition connected MSN to therapy resistance and provided a druggable axis in glioma stem cells.\",\n      \"evidence\": \"MSN KD/OE, Western blot for PI3K/mTOR components, chemoradiotherapy resistance assays, and GNE-317 inhibitor treatment in vitro and in vivo\",\n      \"pmids\": [\"39921260\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"How MSN activates PI3K/mTOR mechanistically not resolved\", \"GNE-317 specificity for MSN not fully established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How MSN's defined membrane-cytoskeleton linker activity (FERM/PIP2/CD44) mechanistically connects to its diverse downstream oncogenic signaling outputs (c-Met, CREB, \\u03b2-catenin, PI3K/mTOR) and to the T-cell defects of immunodeficiency remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No unified mechanism linking membrane scaffolding to nuclear/signaling roles\", \"Substrate or direct binding events for most oncogenic axes undefined\", \"Structure-function link between disease mutations and specific molecular activities not established\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [5]},\n      {\"term_id\": \"GO:0008289\", \"supporting_discovery_ids\": [5]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [0, 5]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [2, 6, 8]},\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CD44\", \"ALK\", \"NONO\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":3,"faith_pct":100.0}}