{"gene":"TMED10","run_date":"2026-06-10T10:51:55","timeline":{"discoveries":[{"year":2011,"finding":"TMED10 (p23/Tmp21) associates with the C1b domain of PKCδ via two key residues (Asp245 and Met266). Silencing TMED10 in LNCaP prostate cancer cells markedly enhanced PKCδ-dependent apoptosis, activation of PKCδ downstream effectors ROCK and JNK by PMA, and translocation of PKCδ to the plasma membrane. A PKCδ mutant unable to interact with p23 triggered strong apoptotic responses, establishing that TMED10 acts as an anchoring protein that retains PKCδ at the perinuclear region and limits its availability for activation.","method":"Yeast two-hybrid, RNAi knockdown in LNCaP cells, site-directed mutagenesis of interaction residues, apoptosis and kinase activation assays","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal yeast two-hybrid plus RNAi knockdown with defined phenotypic readout plus mutagenesis of interaction residues, single lab but multiple orthogonal methods","pmids":["21454541"],"is_preprint":false},{"year":2010,"finding":"TMED10 (p24δ1/TMP21) and p24α2, which both carry dilysine ER-retrieval motifs, co-immunoprecipitate with core components of the γ-secretase complex and the anti-p24α2 immunoprecipitate exhibits γ-secretase activity. Knockdown of p24δ1 or p24α2 increases Aβ generation, and mutational disruption of their dilysine ER-retrieval motifs perturbs inhibition of γ-cleavage. Simultaneous knockdown or co-overexpression of both proteins had no additive effect, suggesting they collaborate in the same pathway to attenuate γ-cleavage of APP without affecting ε-cleavage.","method":"Co-immunoprecipitation, siRNA knockdown, overexpression, dilysine motif mutagenesis, cell-based and cell-free γ-secretase activity assays","journal":"Journal of neurochemistry","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — co-IP with γ-secretase complex showing enzymatic activity, mutagenesis of functional motif, knockdown with defined biochemical phenotype, multiple orthogonal methods in one study","pmids":["20807314"],"is_preprint":false},{"year":2000,"finding":"The p24δ subfamily members Xp24δ1 and Xp24δ2 (orthologues of TMED10/p24delta1) are differentially expressed in Xenopus melanotrope cells; Xp24δ2 expression specifically correlates with proopiomelanocortin (POMC) biosynthetic activity (~25-fold induction during cell activation versus ~2.5-fold for Xp24δ1), indicating a role for the δ subfamily in selective cargo transport in the secretory pathway.","method":"Protein quantification by immunoblot and mRNA quantification by Northern blot during physiological activation, subcellular fractionation","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — quantitative expression and localization with correlation to cargo output, single lab, two methods but no direct functional perturbation of TMED10 specifically","pmids":["10637296"],"is_preprint":false},{"year":2001,"finding":"p24 proteins of the α, β, γ, and δ subfamilies (including the TMED10/p24δ orthologue) are localized to the Golgi in biosynthetically inactive cells, but redistribute to the intermediate compartment and ER exit sites when the cell is highly active. Blocking protein biosynthesis with cycloheximide or dispersing the Golgi with brefeldin A redistributes p24 proteins, demonstrating extensive cycling between ER and Golgi and direct involvement in ER-to-Golgi transport.","method":"Subcellular organelle fractionation, immunofluorescence, pharmacological perturbation (cycloheximide, brefeldin A) in Xenopus melanotrope cells","journal":"The Biochemical journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment with functional consequence, pharmacological perturbation confirms cycling role, single lab with multiple approaches","pmids":["11716771"],"is_preprint":false},{"year":2003,"finding":"Transgene overexpression of p24δ2 (TMED10 orthologue) specifically in Xenopus melanotrope cells displaces all endogenous p24 proteins. Despite a severely distorted p24 system, POMC synthesis is normal but the profile of POMC-derived peptides is altered, impairing background adaptation. This establishes that an intact p24 system (including the δ member) is essential for proper secretory cargo processing.","method":"Cell-specific transgenic overexpression in Xenopus, immunoblot for p24 proteins, quantification of POMC-derived peptides, skin melanophore pigment analysis","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — cell-specific transgenic loss-of-function equivalent with defined secretory pathway phenotype, single lab with multiple orthogonal readouts","pmids":["14699062"],"is_preprint":false},{"year":2007,"finding":"Transgenic expression of p24δ2 (TMED10 orthologue) in Xenopus melanotrope cells does not alter overall ultrastructure or POMC transport/cleavage, but specifically affects Golgi-based processes of POMC glycomaturation and sulfation, demonstrating a role for the δ-subfamily member in Golgi subcompartmental processing rather than ER export. This is distinct from the α-subfamily member, which primarily affects ER-to-Golgi transport.","method":"Melanotrope-specific transgenic expression in Xenopus, electron microscopy, POMC glycosylation and sulfation assays, comparison with p24α transgenic phenotype","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — transgenic loss-of-function approach with biochemical phenotype readout, single lab, multiple orthogonal assays comparing two subfamily members","pmids":["17684551"],"is_preprint":false},{"year":2009,"finding":"COPI- and COPII-binding motifs in p24δ2 (TMED10 orthologue) are required for its Golgi localization and for proper POMC processing. Mutations in either binding motif prevented Golgi localization and caused reduced POMC cleavage, establishing that p24δ fulfils its role in secretory protein biosynthesis through coated transport vesicles.","method":"Stable transgenic expression of COPI- or COPII-binding motif mutants of p24δ2-GFP in Xenopus melanotrope cells, immunofluorescence for Golgi localization, POMC processing assays","journal":"The international journal of biochemistry & cell biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — site-directed mutagenesis of functional motifs with localization and cargo processing readout, single lab, direct functional consequence demonstrated","pmids":["19401156"],"is_preprint":false},{"year":2013,"finding":"In yeast, Erv25 (the p24δ orthologue of TMED10) forms isoform-selective αβγδ heterotetrameric complexes with Emp24 (p24β), and specific p24α and p24γ members. Loss of either Erv25 or Emp24 destabilizes all remaining p24 proteins, producing a null phenotype. Five major α/γ pairs were detected in complexes with Erp25 and Emp24, establishing that the δ-subfamily member is a core structural component of the p24 oligomeric complex required for its stability.","method":"Genetic epistasis (double and triple deletion mutants), co-immunoprecipitation of tagged p24 family members, co-fractionation, localization by fluorescence microscopy","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP plus genetic epistasis with multiple mutant combinations, replicated across multiple isoforms in a single systematic study","pmids":["24217251"],"is_preprint":false},{"year":2000,"finding":"A lumenal coiled-coil heptad-repeat region of yeast Emp24p (p24β) is required for its assembly into p24 complexes containing the δ-subfamily member Erv25p (p24δ, TMED10 orthologue). Chimeric proteins swapping transmembrane/cytosolic domains showed these are dispensable for p24 subfamily-specific oligomerization, pointing to lumenal coiled-coil interactions as the driver of αβγδ heterocomplex assembly.","method":"Domain-swap chimera mutagenesis, in vivo co-immunoprecipitation, functional complementation assays in yeast","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — mutagenesis with functional rescue assay and co-IP, defines domain requirements for complex assembly, single lab with multiple orthogonal methods","pmids":["10722670"],"is_preprint":false},{"year":2023,"finding":"C. elegans TMED genes (including a δ-subfamily member orthologous to TMED10) are required for embryonic viability, animal movement, and vulval morphogenesis. TMED mutants exhibit delayed basement membrane breakdown during vulva development, establishing a specific developmental function for the TMED/p24 family in tissue reorganization. Genetic analysis shows functional redundancy within the γ subfamily but implies that a functional protein from each subfamily, including δ, is required for shared developmental processes.","method":"Loss-of-function mutant analysis, genetic epistasis (double mutants), phenotypic scoring of embryonic viability, movement, vulval morphology, and basement membrane dynamics","journal":"Developmental dynamics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic loss-of-function with defined phenotypic readouts in C. elegans, single lab, multiple phenotypes assessed but TMED10 orthologue not individually isolated from family-wide effects","pmids":["37204056"],"is_preprint":false}],"current_model":"TMED10 (TMP21/p24δ1) is a type-I transmembrane protein of the early secretory pathway that assembles into heterotetrameric αβγδ complexes via lumenal coiled-coil interactions, cycles between the ER and Golgi via COPI/COPII vesicles using dilysine retrieval motifs, and functions both as a regulator of secretory cargo transport and processing (including POMC) and as a modulator of γ-secretase activity—attenuating Aβ generation from APP without affecting ε-cleavage—while also serving as a perinuclear anchor for PKCδ that limits its translocation to the plasma membrane and restrains PKCδ-dependent apoptosis."},"narrative":{"mechanistic_narrative":"TMED10 (p24δ1/TMP21) is a core member of the p24 family of early secretory pathway proteins that organizes cargo transport and processing between the ER and Golgi [PMID:24217251, PMID:11716771]. It is an obligate structural subunit of αβγδ heterotetrameric p24 complexes, whose assembly is driven by lumenal coiled-coil interactions rather than transmembrane or cytosolic domains, and loss of the δ-subfamily member destabilizes the entire p24 oligomer [PMID:24217251, PMID:10722670]. The protein cycles extensively between the ER and Golgi, redistributing between these compartments according to biosynthetic demand and depending on COPI- and COPII-binding motifs for its localization [PMID:11716771, PMID:19401156]. Through this cycling, the δ-subfamily member supports selective secretory cargo handling, specifically contributing to Golgi-based processing of proopiomelanocortin (POMC) including glycomaturation and sulfation, and its proper function is required for normal POMC-derived peptide profiles [PMID:17684551, PMID:14699062, PMID:19401156]. TMED10 also modulates γ-secretase: it co-immunoprecipitates with γ-secretase complex components, and its knockdown or disruption of its dilysine ER-retrieval motif increases Aβ generation, attenuating γ-cleavage of APP without affecting ε-cleavage [PMID:20807314]. Independently, TMED10 acts as a perinuclear anchor for PKCδ, binding the PKCδ C1b domain via Asp245 and Met266 to restrain PKCδ translocation to the plasma membrane and limit PKCδ-dependent apoptosis [PMID:21454541]. The family additionally contributes to developmental tissue reorganization, with TMED/p24 loss delaying basement membrane breakdown during organ morphogenesis [PMID:37204056].","teleology":[{"year":2000,"claim":"Established the structural basis of p24 complex assembly, answering how subfamily-specific αβγδ heterocomplexes containing the δ member form.","evidence":"Domain-swap chimera mutagenesis, in vivo co-IP, and complementation in yeast Emp24p/Erv25p","pmids":["10722670"],"confidence":"High","gaps":["Does not define the stoichiometry or structure of the assembled tetramer","Lumenal coiled-coil interface mapped functionally but not structurally"]},{"year":2000,"claim":"Linked δ-subfamily expression to selective secretory cargo output, raising the idea that p24 proteins serve cargo-specific transport rather than bulk flow.","evidence":"Immunoblot and Northern quantification during melanotrope activation in Xenopus, with fractionation","pmids":["10637296"],"confidence":"Medium","gaps":["Correlative expression, no direct functional perturbation of TMED10 itself","Does not identify the cargo-selectivity mechanism"]},{"year":2001,"claim":"Demonstrated that p24 proteins cycle between ER and Golgi and participate directly in ER-to-Golgi transport, establishing their dynamic itinerary.","evidence":"Fractionation, immunofluorescence, cycloheximide and brefeldin A perturbation in Xenopus melanotropes","pmids":["11716771"],"confidence":"Medium","gaps":["Examines p24 family collectively, not TMED10 specifically","Does not resolve the molecular machinery of the cycling step"]},{"year":2003,"claim":"Showed an intact p24 system including the δ member is required for correct secretory cargo processing, separating cargo synthesis from cargo maturation.","evidence":"Cell-specific transgenic overexpression in Xenopus melanotropes, peptide and pigment phenotyping","pmids":["14699062"],"confidence":"Medium","gaps":["Overexpression displaces all p24 proteins, so the TMED10-specific contribution is not isolated","Mechanism linking p24 disruption to altered peptide profile unresolved"]},{"year":2007,"claim":"Localized the δ-subfamily function to Golgi subcompartmental processing (glycomaturation, sulfation), distinguishing it from α-subfamily ER-export roles.","evidence":"Melanotrope-specific transgenics in Xenopus, EM, POMC glycosylation/sulfation assays vs p24α","pmids":["17684551"],"confidence":"Medium","gaps":["Does not show how δ member directs Golgi enzymes to cargo","Phenotype derived from transgenic perturbation, not endogenous TMED10 loss"]},{"year":2009,"claim":"Established that COPI- and COPII-binding motifs are mechanistically required for δ-subfamily Golgi localization and cargo processing, tying transport-machinery engagement to function.","evidence":"Transgenic COPI/COPII motif mutants of p24δ2-GFP in Xenopus, localization and POMC processing assays","pmids":["19401156"],"confidence":"Medium","gaps":["Performed on Xenopus orthologue, not human TMED10","Does not quantify coat-protein binding affinities directly"]},{"year":2010,"claim":"Identified TMED10 as a modulator of γ-secretase that selectively attenuates Aβ generation, connecting the p24 system to APP processing.","evidence":"Co-IP with γ-secretase, siRNA knockdown, dilysine motif mutagenesis, cell-based and cell-free activity assays","pmids":["20807314"],"confidence":"High","gaps":["Does not resolve whether TMED10 contacts γ-secretase directly or via the broader complex","Structural basis for γ- vs ε-cleavage selectivity unknown"]},{"year":2011,"claim":"Defined a non-secretory role: TMED10 anchors PKCδ at the perinuclear region via specific residues, restraining its activation and apoptotic signaling.","evidence":"Yeast two-hybrid, RNAi in LNCaP, interaction-residue mutagenesis, apoptosis and kinase activation assays","pmids":["21454541"],"confidence":"High","gaps":["Does not connect the PKCδ-anchoring role to TMED10's secretory pathway functions","Generality beyond prostate cancer cells untested"]},{"year":2013,"claim":"Confirmed the δ-subfamily member as an indispensable structural core of the p24 complex whose loss destabilizes all partners, formalizing the heterotetramer architecture.","evidence":"Genetic epistasis with double/triple deletions, reciprocal Co-IP, co-fractionation in yeast (Erv25/Emp24)","pmids":["24217251"],"confidence":"High","gaps":["Defined in yeast; complex composition in human cells not directly addressed here","Does not map which cargoes each α/γ pairing selects"]},{"year":2023,"claim":"Extended p24/TMED function to development, showing the family is required for tissue reorganization including basement membrane breakdown.","evidence":"Loss-of-function and double-mutant analysis in C. elegans with developmental phenotyping","pmids":["37204056"],"confidence":"Medium","gaps":["TMED10 orthologue not isolated from family-wide effects","Molecular cargo underlying basement membrane defect unidentified"]},{"year":null,"claim":"How TMED10's distinct activities—p24 complex cargo transport, γ-secretase modulation, and PKCδ anchoring—are coordinated or regulated within a single cell remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unifying model linking secretory and signaling roles","Human structural data on p24 heterotetramer absent from corpus","Cargo selectivity determinants for human TMED10 not defined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[1]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,1]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[7,8]},{"term_id":"GO:0038024","term_label":"cargo receptor activity","supporting_discovery_ids":[4,5,6]}],"localization":[{"term_id":"GO:0005794","term_label":"Golgi apparatus","supporting_discovery_ids":[3,5,6]},{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[1,3]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[3,6]},{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[4,5]},{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[3,6]}],"complexes":["p24 αβγδ heterotetrameric complex","γ-secretase complex"],"partners":["PRKCD","TMED2","EMP24","ERV25"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P49755","full_name":"Transmembrane emp24 domain-containing protein 10","aliases":["21 kDa transmembrane-trafficking protein","S31I125","S31III125","Tmp-21-I","Transmembrane protein Tmp21","p23","p24 family protein delta-1","p24delta1","p24delta"],"length_aa":219,"mass_kda":25.0,"function":"Cargo receptor involved in protein vesicular trafficking and quality control in the endoplasmic reticulum (ER) and Golgi (PubMed:10052452, PubMed:11726511, PubMed:16641999, PubMed:17288597, PubMed:19296914, PubMed:20427317, PubMed:21219331, PubMed:27569046). The p24 protein family is a group of transmembrane proteins that bind coat protein complex I/COPI and coat protein complex II/COPII involved in vesicular trafficking between the membranes (PubMed:10052452). Acts at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and involved in vesicle coat formation at the cytoplasmic side (PubMed:20427317, PubMed:27569046). Mainly functions in the early secretory pathway and cycles between the ER, ER-Golgi intermediate compartment (ERGIC) and Golgi, mediating cargo transport through COPI and COPII-coated vesicles (PubMed:10052452, PubMed:10852829, PubMed:12237308). In COPII vesicle-mediated anterograde transport, involved in the transport of GPI-anchored proteins by acting together with TMED2 as their cargo receptor; the function specifically implies SEC24C and SEC24D of the COPII vesicle coat and lipid raft-like microdomains of the ER (PubMed:20427317, PubMed:27569046). Recognizes GPI anchors structural remodeled in the ER by the GPI inositol-deacylase/PGAP1 and the metallophosphoesterase MPPE1/PGAP5 (By similarity). In COPI vesicle-mediated retrograde transport, involved in the biogenesis of COPI vesicles and vesicle coat recruitment (PubMed:11726511). Involved in trafficking of amyloid beta A4 protein and soluble APP-beta release (independent from the modulation of gamma-secretase activity) (PubMed:17288597). Involved in the KDELR2-mediated retrograde transport of the toxin A subunit (CTX-A-K63)together with COPI and the COOH terminus of KDELR2 (By similarity). On Golgi membranes, acts as a primary receptor for ARF1-GDP, a GTP-binding protein involved in COPI-vesicle formation (PubMed:11726511). Increases coatomer-dependent GTPase-activating activity of ARFGAP2 which mediates the hydrolysis of ARF1-bound GTP and therefore modulates protein trafficking from the Golgi apparatus (PubMed:19296914). Involved in the exocytic trafficking of G protein-coupled receptors F2LR1/PAR2 (trypsin and tryspin-like enzyme receptor), OPRM1 (opioid receptor) and P2RY4 (UTD and UDP receptor) from the Golgi to the plasma membrane, thus contributing to receptor resensitization (PubMed:21219331). In addition to its cargo receptor activity, may also act as a protein channel after oligomerization, facilitating the post-translational entry of leaderless cytoplasmic cargo into the ERGIC (PubMed:32272059). Involved in the translocation into ERGIC, the vesicle entry and the secretion of leaderless cargos (lacking the secretion signal sequence), including the mature form of interleukin 1/IL-1 family members, the alpha-crystallin B chain HSPB5, the carbohydrate-binding proteins galectin-1/LGALS1 and galectin-3/LGALS3, the microtubule-associated protein Tau/MAPT, and the annexin A1/ANXA1; the translocation process is dependent on cargo protein unfolding and enhanced by chaperones HSP90AB1 and HSP90B1/GRP9 (PubMed:32272059). Could also associates with the presenilin-dependent gamma-secretase complex in order to regulate gamma-cleavages of the amyloid beta A4 protein to yield amyloid-beta 40/Abeta40 (PubMed:16641999)","subcellular_location":"Endoplasmic reticulum membrane; Endoplasmic reticulum-Golgi intermediate compartment membrane; Golgi apparatus membrane; Golgi apparatus, cis-Golgi network membrane; Golgi apparatus, trans-Golgi network membrane; Cytoplasmic vesicle, secretory vesicle membrane; Cell membrane; Melanosome","url":"https://www.uniprot.org/uniprotkb/P49755/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TMED10","classification":"Not Classified","n_dependent_lines":691,"n_total_lines":1208,"dependency_fraction":0.5720198675496688},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000170348","cell_line_id":"CID000906","localizations":[{"compartment":"er","grade":3},{"compartment":"vesicles","grade":3},{"compartment":"golgi","grade":2}],"interactors":[{"gene":"GORASP2","stoichiometry":10.0},{"gene":"NOLC1","stoichiometry":10.0},{"gene":"TMED4","stoichiometry":10.0},{"gene":"TMED2","stoichiometry":10.0},{"gene":"TMED1","stoichiometry":10.0},{"gene":"TMED7-TICAM2;TMED7","stoichiometry":10.0},{"gene":"COPA","stoichiometry":4.0},{"gene":"MIF","stoichiometry":4.0},{"gene":"TMED3","stoichiometry":4.0},{"gene":"EMD","stoichiometry":4.0}],"url":"https://opencell.sf.czbiohub.org/target/CID000906","total_profiled":1310},"omim":[{"mim_id":"620437","title":"TRANSMEMBRANE p24 TRAFFICKING PROTEIN 3; TMED3","url":"https://www.omim.org/entry/620437"},{"mim_id":"620436","title":"TRANSMEMBRANE p24 TRAFFICKING PROTEIN 9; TMED9","url":"https://www.omim.org/entry/620436"},{"mim_id":"619990","title":"TRANSMEMBRANE p24 TRAFFICKING PROTEIN 7; TMED7","url":"https://www.omim.org/entry/619990"},{"mim_id":"619642","title":"TRANSMEMBRANE p24 TRAFFICKING PROTEIN 2; TMED2","url":"https://www.omim.org/entry/619642"},{"mim_id":"605406","title":"TRANSMEMBRANE p24 TRAFFICKING PROTEIN 10; TMED10","url":"https://www.omim.org/entry/605406"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Golgi apparatus","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TMED10"},"hgnc":{"alias_symbol":["TMP21","P24(DELTA)","p24d1","p24delta1","p23"],"prev_symbol":[]},"alphafold":{"accession":"P49755","domains":[{"cath_id":"2.60.120.680","chopping":"29-132","consensus_level":"medium","plddt":89.939,"start":29,"end":132}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P49755","model_url":"https://alphafold.ebi.ac.uk/files/AF-P49755-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P49755-F1-predicted_aligned_error_v6.png","plddt_mean":87.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TMED10","jax_strain_url":"https://www.jax.org/strain/search?query=TMED10"},"sequence":{"accession":"P49755","fasta_url":"https://rest.uniprot.org/uniprotkb/P49755.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P49755/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P49755"}},"corpus_meta":[{"pmid":"3701932","id":"PMC_3701932","title":"Hepatitis delta virus: protein composition of delta antigen and its hepatitis B virus-derived envelope.","date":"1986","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/3701932","citation_count":265,"is_preprint":false},{"pmid":"2447291","id":"PMC_2447291","title":"A single antigenomic open reading frame of the hepatitis delta virus encodes the epitope(s) of both hepatitis delta antigen polypeptides p24 delta and p27 delta.","date":"1988","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/2447291","citation_count":201,"is_preprint":false},{"pmid":"7037069","id":"PMC_7037069","title":"The phenotype of the neoplastic cells of hairy cell leukemia studied with monoclonal antibodies.","date":"1982","source":"Blood","url":"https://pubmed.ncbi.nlm.nih.gov/7037069","citation_count":165,"is_preprint":false},{"pmid":"1825186","id":"PMC_1825186","title":"A subset of gamma delta lymphocytes is increased during HIV-1 infection.","date":"1991","source":"Clinical and experimental immunology","url":"https://pubmed.ncbi.nlm.nih.gov/1825186","citation_count":155,"is_preprint":false},{"pmid":"7526538","id":"PMC_7526538","title":"Complement control proteins, CD46, CD55, and CD59, as common surface constituents of human and simian immunodeficiency viruses and possible targets for vaccine protection.","date":"1994","source":"Virology","url":"https://pubmed.ncbi.nlm.nih.gov/7526538","citation_count":114,"is_preprint":false},{"pmid":"9110071","id":"PMC_9110071","title":"Mitochondria alterations and dramatic tendency to undergo apoptosis in peripheral blood lymphocytes during acute HIV syndrome.","date":"1997","source":"AIDS (London, England)","url":"https://pubmed.ncbi.nlm.nih.gov/9110071","citation_count":112,"is_preprint":false},{"pmid":"10438380","id":"PMC_10438380","title":"Phosphoantigen-reactive Vgamma9Vdelta2 T lymphocytes suppress in vitro human immunodeficiency virus type 1 replication by cell-released antiviral factors including CC chemokines.","date":"1999","source":"The Journal of infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/10438380","citation_count":103,"is_preprint":false},{"pmid":"9329513","id":"PMC_9329513","title":"HIV-1 viral load, phenotype, and resistance in a subset of drug-naive participants from the Delta trial. The National Virology Groups. Delta Virology Working Group and Coordinating Committee.","date":"1997","source":"Lancet (London, England)","url":"https://pubmed.ncbi.nlm.nih.gov/9329513","citation_count":101,"is_preprint":false},{"pmid":"9412701","id":"PMC_9412701","title":"Increased frequency of CCR-5 delta 32 heterozygotes among long-term non-progressors with HIV-1 infection. The Australian Long-Term Non-Progressor Study Group.","date":"1997","source":"AIDS (London, England)","url":"https://pubmed.ncbi.nlm.nih.gov/9412701","citation_count":95,"is_preprint":false},{"pmid":"19625466","id":"PMC_19625466","title":"Hepatitis delta virus proteins repress hepatitis B virus enhancers and activate the alpha/beta interferon-inducible MxA gene.","date":"2009","source":"The Journal of general virology","url":"https://pubmed.ncbi.nlm.nih.gov/19625466","citation_count":83,"is_preprint":false},{"pmid":"9132281","id":"PMC_9132281","title":"Functional gamma delta T-lymphocyte defect associated with human immunodeficiency virus infections.","date":"1997","source":"Molecular medicine (Cambridge, Mass.)","url":"https://pubmed.ncbi.nlm.nih.gov/9132281","citation_count":70,"is_preprint":false},{"pmid":"12972507","id":"PMC_12972507","title":"Selective inactivation of CCR5 and decreased infectivity of R5 HIV-1 strains mediated by opioid-induced heterologous 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Supplementum","url":"https://pubmed.ncbi.nlm.nih.gov/8260879","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":45593,"output_tokens":3409,"usd":0.093957,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10673,"output_tokens":3547,"usd":0.07102,"stage2_stop_reason":"end_turn"},"total_usd":0.164977,"stage1_batch_id":"msgbatch_017qqVz33Ga63SCDwzb35XPb","stage2_batch_id":"msgbatch_01Scr2Ei9x4HJMiRGxwrmvLK","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking at the 86 papers, I need to identify which ones are actually about TMED10 (also known as TMP21, p24delta1, p24d1, p24(delta)). \n\nThe vast majority of papers are about:\n- Hepatitis Delta Virus antigens (p24/p27) - NOT TMED10\n- HIV-related p24 (HIV capsid protein) - NOT TMED10\n- CCR5 delta32 mutation - NOT TMED10\n- Various delta-related topics unrelated to TMED10\n\nThe relevant papers for TMED10 (p24 family cargo receptors in the secretory pathway) are papers [18], [21], [24], [28], [29], [39], [44], [46], [47], [50], [52], [54], [59], [65], [69], [77].\n\nPaper [24] is specifically about p23/Tmp21 (TMED10 alias) and PKCδ interaction.\nPaper [59] mentions TMP21/p24δ(1) modulating γ-secretase/APP processing.\nPapers [18], [21], [28], [29], [39], [44], [46], [47], [50], [52], [54], [65], [69], [77] are about the p24/TMED family broadly, with some specifically addressing the delta subfamily member that is TMED10's ortholog.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2011,\n      \"finding\": \"TMED10 (p23/Tmp21) associates with the C1b domain of PKCδ via two key residues (Asp245 and Met266). Silencing TMED10 in LNCaP prostate cancer cells markedly enhanced PKCδ-dependent apoptosis, activation of PKCδ downstream effectors ROCK and JNK by PMA, and translocation of PKCδ to the plasma membrane. A PKCδ mutant unable to interact with p23 triggered strong apoptotic responses, establishing that TMED10 acts as an anchoring protein that retains PKCδ at the perinuclear region and limits its availability for activation.\",\n      \"method\": \"Yeast two-hybrid, RNAi knockdown in LNCaP cells, site-directed mutagenesis of interaction residues, apoptosis and kinase activation assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal yeast two-hybrid plus RNAi knockdown with defined phenotypic readout plus mutagenesis of interaction residues, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"21454541\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"TMED10 (p24δ1/TMP21) and p24α2, which both carry dilysine ER-retrieval motifs, co-immunoprecipitate with core components of the γ-secretase complex and the anti-p24α2 immunoprecipitate exhibits γ-secretase activity. Knockdown of p24δ1 or p24α2 increases Aβ generation, and mutational disruption of their dilysine ER-retrieval motifs perturbs inhibition of γ-cleavage. Simultaneous knockdown or co-overexpression of both proteins had no additive effect, suggesting they collaborate in the same pathway to attenuate γ-cleavage of APP without affecting ε-cleavage.\",\n      \"method\": \"Co-immunoprecipitation, siRNA knockdown, overexpression, dilysine motif mutagenesis, cell-based and cell-free γ-secretase activity assays\",\n      \"journal\": \"Journal of neurochemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — co-IP with γ-secretase complex showing enzymatic activity, mutagenesis of functional motif, knockdown with defined biochemical phenotype, multiple orthogonal methods in one study\",\n      \"pmids\": [\"20807314\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2000,\n      \"finding\": \"The p24δ subfamily members Xp24δ1 and Xp24δ2 (orthologues of TMED10/p24delta1) are differentially expressed in Xenopus melanotrope cells; Xp24δ2 expression specifically correlates with proopiomelanocortin (POMC) biosynthetic activity (~25-fold induction during cell activation versus ~2.5-fold for Xp24δ1), indicating a role for the δ subfamily in selective cargo transport in the secretory pathway.\",\n      \"method\": \"Protein quantification by immunoblot and mRNA quantification by Northern blot during physiological activation, subcellular fractionation\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — quantitative expression and localization with correlation to cargo output, single lab, two methods but no direct functional perturbation of TMED10 specifically\",\n      \"pmids\": [\"10637296\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"p24 proteins of the α, β, γ, and δ subfamilies (including the TMED10/p24δ orthologue) are localized to the Golgi in biosynthetically inactive cells, but redistribute to the intermediate compartment and ER exit sites when the cell is highly active. Blocking protein biosynthesis with cycloheximide or dispersing the Golgi with brefeldin A redistributes p24 proteins, demonstrating extensive cycling between ER and Golgi and direct involvement in ER-to-Golgi transport.\",\n      \"method\": \"Subcellular organelle fractionation, immunofluorescence, pharmacological perturbation (cycloheximide, brefeldin A) in Xenopus melanotrope cells\",\n      \"journal\": \"The Biochemical journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiment with functional consequence, pharmacological perturbation confirms cycling role, single lab with multiple approaches\",\n      \"pmids\": [\"11716771\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"Transgene overexpression of p24δ2 (TMED10 orthologue) specifically in Xenopus melanotrope cells displaces all endogenous p24 proteins. Despite a severely distorted p24 system, POMC synthesis is normal but the profile of POMC-derived peptides is altered, impairing background adaptation. This establishes that an intact p24 system (including the δ member) is essential for proper secretory cargo processing.\",\n      \"method\": \"Cell-specific transgenic overexpression in Xenopus, immunoblot for p24 proteins, quantification of POMC-derived peptides, skin melanophore pigment analysis\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — cell-specific transgenic loss-of-function equivalent with defined secretory pathway phenotype, single lab with multiple orthogonal readouts\",\n      \"pmids\": [\"14699062\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2007,\n      \"finding\": \"Transgenic expression of p24δ2 (TMED10 orthologue) in Xenopus melanotrope cells does not alter overall ultrastructure or POMC transport/cleavage, but specifically affects Golgi-based processes of POMC glycomaturation and sulfation, demonstrating a role for the δ-subfamily member in Golgi subcompartmental processing rather than ER export. This is distinct from the α-subfamily member, which primarily affects ER-to-Golgi transport.\",\n      \"method\": \"Melanotrope-specific transgenic expression in Xenopus, electron microscopy, POMC glycosylation and sulfation assays, comparison with p24α transgenic phenotype\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — transgenic loss-of-function approach with biochemical phenotype readout, single lab, multiple orthogonal assays comparing two subfamily members\",\n      \"pmids\": [\"17684551\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"COPI- and COPII-binding motifs in p24δ2 (TMED10 orthologue) are required for its Golgi localization and for proper POMC processing. Mutations in either binding motif prevented Golgi localization and caused reduced POMC cleavage, establishing that p24δ fulfils its role in secretory protein biosynthesis through coated transport vesicles.\",\n      \"method\": \"Stable transgenic expression of COPI- or COPII-binding motif mutants of p24δ2-GFP in Xenopus melanotrope cells, immunofluorescence for Golgi localization, POMC processing assays\",\n      \"journal\": \"The international journal of biochemistry & cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — site-directed mutagenesis of functional motifs with localization and cargo processing readout, single lab, direct functional consequence demonstrated\",\n      \"pmids\": [\"19401156\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"In yeast, Erv25 (the p24δ orthologue of TMED10) forms isoform-selective αβγδ heterotetrameric complexes with Emp24 (p24β), and specific p24α and p24γ members. Loss of either Erv25 or Emp24 destabilizes all remaining p24 proteins, producing a null phenotype. Five major α/γ pairs were detected in complexes with Erp25 and Emp24, establishing that the δ-subfamily member is a core structural component of the p24 oligomeric complex required for its stability.\",\n      \"method\": \"Genetic epistasis (double and triple deletion mutants), co-immunoprecipitation of tagged p24 family members, co-fractionation, localization by fluorescence microscopy\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP plus genetic epistasis with multiple mutant combinations, replicated across multiple isoforms in a single systematic study\",\n      \"pmids\": [\"24217251\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2000,\n      \"finding\": \"A lumenal coiled-coil heptad-repeat region of yeast Emp24p (p24β) is required for its assembly into p24 complexes containing the δ-subfamily member Erv25p (p24δ, TMED10 orthologue). Chimeric proteins swapping transmembrane/cytosolic domains showed these are dispensable for p24 subfamily-specific oligomerization, pointing to lumenal coiled-coil interactions as the driver of αβγδ heterocomplex assembly.\",\n      \"method\": \"Domain-swap chimera mutagenesis, in vivo co-immunoprecipitation, functional complementation assays in yeast\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — mutagenesis with functional rescue assay and co-IP, defines domain requirements for complex assembly, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"10722670\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"C. elegans TMED genes (including a δ-subfamily member orthologous to TMED10) are required for embryonic viability, animal movement, and vulval morphogenesis. TMED mutants exhibit delayed basement membrane breakdown during vulva development, establishing a specific developmental function for the TMED/p24 family in tissue reorganization. Genetic analysis shows functional redundancy within the γ subfamily but implies that a functional protein from each subfamily, including δ, is required for shared developmental processes.\",\n      \"method\": \"Loss-of-function mutant analysis, genetic epistasis (double mutants), phenotypic scoring of embryonic viability, movement, vulval morphology, and basement membrane dynamics\",\n      \"journal\": \"Developmental dynamics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic loss-of-function with defined phenotypic readouts in C. elegans, single lab, multiple phenotypes assessed but TMED10 orthologue not individually isolated from family-wide effects\",\n      \"pmids\": [\"37204056\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TMED10 (TMP21/p24δ1) is a type-I transmembrane protein of the early secretory pathway that assembles into heterotetrameric αβγδ complexes via lumenal coiled-coil interactions, cycles between the ER and Golgi via COPI/COPII vesicles using dilysine retrieval motifs, and functions both as a regulator of secretory cargo transport and processing (including POMC) and as a modulator of γ-secretase activity—attenuating Aβ generation from APP without affecting ε-cleavage—while also serving as a perinuclear anchor for PKCδ that limits its translocation to the plasma membrane and restrains PKCδ-dependent apoptosis.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TMED10 (p24\\u03b41/TMP21) is a core member of the p24 family of early secretory pathway proteins that organizes cargo transport and processing between the ER and Golgi [#7, #3]. It is an obligate structural subunit of \\u03b1\\u03b2\\u03b3\\u03b4 heterotetrameric p24 complexes, whose assembly is driven by lumenal coiled-coil interactions rather than transmembrane or cytosolic domains, and loss of the \\u03b4-subfamily member destabilizes the entire p24 oligomer [#7, #8]. The protein cycles extensively between the ER and Golgi, redistributing between these compartments according to biosynthetic demand and depending on COPI- and COPII-binding motifs for its localization [#3, #6]. Through this cycling, the \\u03b4-subfamily member supports selective secretory cargo handling, specifically contributing to Golgi-based processing of proopiomelanocortin (POMC) including glycomaturation and sulfation, and its proper function is required for normal POMC-derived peptide profiles [#5, #4, #6]. TMED10 also modulates \\u03b3-secretase: it co-immunoprecipitates with \\u03b3-secretase complex components, and its knockdown or disruption of its dilysine ER-retrieval motif increases A\\u03b2 generation, attenuating \\u03b3-cleavage of APP without affecting \\u03b5-cleavage [#1]. Independently, TMED10 acts as a perinuclear anchor for PKC\\u03b4, binding the PKC\\u03b4 C1b domain via Asp245 and Met266 to restrain PKC\\u03b4 translocation to the plasma membrane and limit PKC\\u03b4-dependent apoptosis [#0]. The family additionally contributes to developmental tissue reorganization, with TMED/p24 loss delaying basement membrane breakdown during organ morphogenesis [#9].\",\n  \"teleology\": [\n    {\n      \"year\": 2000,\n      \"claim\": \"Established the structural basis of p24 complex assembly, answering how subfamily-specific \\u03b1\\u03b2\\u03b3\\u03b4 heterocomplexes containing the \\u03b4 member form.\",\n      \"evidence\": \"Domain-swap chimera mutagenesis, in vivo co-IP, and complementation in yeast Emp24p/Erv25p\",\n      \"pmids\": [\"10722670\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not define the stoichiometry or structure of the assembled tetramer\", \"Lumenal coiled-coil interface mapped functionally but not structurally\"]\n    },\n    {\n      \"year\": 2000,\n      \"claim\": \"Linked \\u03b4-subfamily expression to selective secretory cargo output, raising the idea that p24 proteins serve cargo-specific transport rather than bulk flow.\",\n      \"evidence\": \"Immunoblot and Northern quantification during melanotrope activation in Xenopus, with fractionation\",\n      \"pmids\": [\"10637296\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Correlative expression, no direct functional perturbation of TMED10 itself\", \"Does not identify the cargo-selectivity mechanism\"]\n    },\n    {\n      \"year\": 2001,\n      \"claim\": \"Demonstrated that p24 proteins cycle between ER and Golgi and participate directly in ER-to-Golgi transport, establishing their dynamic itinerary.\",\n      \"evidence\": \"Fractionation, immunofluorescence, cycloheximide and brefeldin A perturbation in Xenopus melanotropes\",\n      \"pmids\": [\"11716771\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Examines p24 family collectively, not TMED10 specifically\", \"Does not resolve the molecular machinery of the cycling step\"]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"Showed an intact p24 system including the \\u03b4 member is required for correct secretory cargo processing, separating cargo synthesis from cargo maturation.\",\n      \"evidence\": \"Cell-specific transgenic overexpression in Xenopus melanotropes, peptide and pigment phenotyping\",\n      \"pmids\": [\"14699062\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Overexpression displaces all p24 proteins, so the TMED10-specific contribution is not isolated\", \"Mechanism linking p24 disruption to altered peptide profile unresolved\"]\n    },\n    {\n      \"year\": 2007,\n      \"claim\": \"Localized the \\u03b4-subfamily function to Golgi subcompartmental processing (glycomaturation, sulfation), distinguishing it from \\u03b1-subfamily ER-export roles.\",\n      \"evidence\": \"Melanotrope-specific transgenics in Xenopus, EM, POMC glycosylation/sulfation assays vs p24\\u03b1\",\n      \"pmids\": [\"17684551\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not show how \\u03b4 member directs Golgi enzymes to cargo\", \"Phenotype derived from transgenic perturbation, not endogenous TMED10 loss\"]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Established that COPI- and COPII-binding motifs are mechanistically required for \\u03b4-subfamily Golgi localization and cargo processing, tying transport-machinery engagement to function.\",\n      \"evidence\": \"Transgenic COPI/COPII motif mutants of p24\\u03b42-GFP in Xenopus, localization and POMC processing assays\",\n      \"pmids\": [\"19401156\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Performed on Xenopus orthologue, not human TMED10\", \"Does not quantify coat-protein binding affinities directly\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Identified TMED10 as a modulator of \\u03b3-secretase that selectively attenuates A\\u03b2 generation, connecting the p24 system to APP processing.\",\n      \"evidence\": \"Co-IP with \\u03b3-secretase, siRNA knockdown, dilysine motif mutagenesis, cell-based and cell-free activity assays\",\n      \"pmids\": [\"20807314\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not resolve whether TMED10 contacts \\u03b3-secretase directly or via the broader complex\", \"Structural basis for \\u03b3- vs \\u03b5-cleavage selectivity unknown\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Defined a non-secretory role: TMED10 anchors PKC\\u03b4 at the perinuclear region via specific residues, restraining its activation and apoptotic signaling.\",\n      \"evidence\": \"Yeast two-hybrid, RNAi in LNCaP, interaction-residue mutagenesis, apoptosis and kinase activation assays\",\n      \"pmids\": [\"21454541\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not connect the PKC\\u03b4-anchoring role to TMED10's secretory pathway functions\", \"Generality beyond prostate cancer cells untested\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Confirmed the \\u03b4-subfamily member as an indispensable structural core of the p24 complex whose loss destabilizes all partners, formalizing the heterotetramer architecture.\",\n      \"evidence\": \"Genetic epistasis with double/triple deletions, reciprocal Co-IP, co-fractionation in yeast (Erv25/Emp24)\",\n      \"pmids\": [\"24217251\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Defined in yeast; complex composition in human cells not directly addressed here\", \"Does not map which cargoes each \\u03b1/\\u03b3 pairing selects\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Extended p24/TMED function to development, showing the family is required for tissue reorganization including basement membrane breakdown.\",\n      \"evidence\": \"Loss-of-function and double-mutant analysis in C. elegans with developmental phenotyping\",\n      \"pmids\": [\"37204056\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"TMED10 orthologue not isolated from family-wide effects\", \"Molecular cargo underlying basement membrane defect unidentified\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TMED10's distinct activities\\u2014p24 complex cargo transport, \\u03b3-secretase modulation, and PKC\\u03b4 anchoring\\u2014are coordinated or regulated within a single cell remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No unifying model linking secretory and signaling roles\", \"Human structural data on p24 heterotetramer absent from corpus\", \"Cargo selectivity determinants for human TMED10 not defined\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [7, 8]},\n      {\"term_id\": \"GO:0038024\", \"supporting_discovery_ids\": [4, 5, 6]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [3, 5, 6]},\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [3, 6]},\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [4, 5]},\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [3, 6]}\n    ],\n    \"complexes\": [\"p24 \\u03b1\\u03b2\\u03b3\\u03b4 heterotetrameric complex\", \"\\u03b3-secretase complex\"],\n    \"partners\": [\"PRKCD\", \"TMED2\", \"EMP24\", \"ERV25\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":7,"faith_pct":85.71428571428571}}