{"gene":"ECD","run_date":"2026-06-09T23:54:42","timeline":{"discoveries":[{"year":2021,"finding":"Drosophila Ecdysoneless (Ecd) promotes U5 snRNP assembly and stabilizes Prp8 protein. Ecd delivers Prp8 to the emerging U5 snRNPs in the cytoplasm; Ecd deficiency leads to reduced Prp8 protein levels and compromised U5 snRNP biogenesis, causing loss of splicing fidelity. SmD3 was identified as a novel interaction partner of Ecd by proteomic approaches.","method":"Drosophila genetics, proteomic approaches (Co-IP/MS), loss-of-function with splicing fidelity readout","journal":"Nucleic Acids Research","confidence":"High","confidence_rationale":"Tier 2 / Strong — Drosophila genetic loss-of-function combined with proteomic identification of interaction partners and defined molecular phenotype (Prp8 destabilization, U5 snRNP biogenesis failure, splicing defects), multiple orthogonal methods in single study","pmids":["33444449"],"is_preprint":false},{"year":2015,"finding":"Mammalian ECD interacts with the R2TP cochaperone complex component RUVBL1 in a phosphorylation-independent manner, and this interaction is essential for ECD's cell cycle progression function. ECD also undergoes CK2-mediated phosphorylation that facilitates interaction with PIH1D1 (another R2TP component), but phosphorylation-deficient ECD mutants that lose PIH1D1 binding still interact with R2TP and partially retain cell cycle function. The RUVBL1 interaction is the key functional determinant for rescuing Ecd-deficient cells from cell cycle arrest.","method":"Biochemical Co-IP, in vitro binding assays with phosphorylation-deficient mutants, rescue of Ecd-KO cells with mutant constructs","journal":"Molecular and Cellular Biology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal biochemical interaction mapping with mutagenesis, functional rescue assays in Ecd-deficient cells, two orthogonal methods in a single rigorous study","pmids":["26711270"],"is_preprint":false},{"year":2017,"finding":"Mammalian ECD is a negative regulator of the PERK arm of the unfolded protein response (UPR). ECD colocalizes and coimmunoprecipitates with PERK and GRP78. ECD depletion increases phospho-PERK and phospho-eIF2α levels; ECD overexpression decreases p-PERK, p-eIF2α, and ATF4 but increases GRP78 protein (without increasing GRP78 mRNA, suggesting posttranslational regulation). Knockdown of GRP78 reverses ECD's attenuation of PERK signaling. ECD overexpression confers survival advantage under ER stress.","method":"Co-immunoprecipitation, colocalization, siRNA knockdown, overexpression, immunoblot for pathway components, GRP78 knockdown epistasis","journal":"Molecular and Cellular Biology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP, epistasis (GRP78 KD reversal), loss- and gain-of-function with defined pathway readouts, multiple orthogonal methods in single study","pmids":["28652267"],"is_preprint":false},{"year":2018,"finding":"ECD promotes gastric cancer invasion and metastasis by protecting hnRNP F from ubiquitination and proteasomal degradation. ZFP91 was identified as the E3 ubiquitin ligase responsible for hnRNP F ubiquitination at Lys185. ECD competitively binds hnRNP F via its N-terminal STG1 domain (residues 13–383), preventing hnRNP F from interacting with ZFP91, thus blocking ZFP91-mediated ubiquitination and degradation of hnRNP F.","method":"Co-IP, domain mapping with truncation mutants, ubiquitination assay, proteasome inhibitor experiments, siRNA knockdown, in vitro invasion/migration assays, in vivo metastasis model","journal":"Cell Death & Disease","confidence":"High","confidence_rationale":"Tier 2 / Moderate — Co-IP with domain mapping, in vitro ubiquitination assay, functional rescue/epistasis with defined molecular mechanism, multiple orthogonal methods","pmids":["29706618"],"is_preprint":false},{"year":2015,"finding":"In gastric cancer, ACK1 activates AKT (phosphorylation at Thr308 and Ser473), which upregulates the transcription factor POU2F1; POU2F1 directly binds the promoter of ECD and transcriptionally activates ECD expression. ECD overexpression downstream of this pathway promotes EMT, migration, and invasion. Silencing ECD completely blocks ACK1-overexpression-induced EMT, migration, and invasion, placing ECD as a functional effector in the ACK1-AKT-POU2F1-ECD signaling axis.","method":"SILAC quantitative proteomics, siRNA knockdown, chromatin immunoprecipitation (POU2F1 on ECD promoter), overexpression, in vitro migration/invasion, in vivo metastasis","journal":"The Journal of Pathology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — SILAC proteomics, ChIP validation of promoter binding, genetic epistasis by siRNA, multiple orthogonal methods in single study","pmids":["25678401"],"is_preprint":false},{"year":2017,"finding":"ECD promotes gastric cancer tumorigenesis via ubiquitination and degradation of the tumor suppressor p53. Overexpression of ECD or ACK1 promotes p53 ubiquitination and decreases p53 levels; silencing of ECD decreases p53 ubiquitination and increases p53 levels. Silencing ECD attenuates the enhancement of p53 ubiquitination induced by ACK1 overexpression, placing ECD downstream of ACK1 in controlling p53 stability.","method":"Ubiquitination assay, siRNA knockdown, overexpression, immunoblot, colony formation and cell cycle assays","journal":"Oncotarget","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — ubiquitination assay and epistasis experiments, but single lab and the direct E3/E2 machinery used by ECD for p53 ubiquitination was not identified in this study","pmids":["26498357"],"is_preprint":false},{"year":1993,"finding":"The Drosophila ecdysoneless (ecd) locus is required for embryonic development, successful completion of each larval molt, adult eclosion, and female fertility. Mutant allele analysis showed ecd is required for normal macrochaete differentiation. Gene dosage and complementation studies with five nonconditional lethal alleles established that ecd plays both prezygotic and postzygotic roles essential for normal development. Severity of phenotype correlated with ecd mutant genotype.","method":"Drosophila genetics — gene dosage, complementation tests, phenotypic analysis of multiple alleles","journal":"Developmental Genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — systematic genetic analysis with multiple alleles across developmental stages, single lab but comprehensive allelic series","pmids":["8293578"],"is_preprint":false},{"year":1984,"finding":"The Drosophila temperature-sensitive l(3)ecd-1ts mutation causes an ecdysteroid deficit at the restrictive temperature (29°C), blocking pupariation. HPLC and RIA analyses confirmed low ecdysteroid levels in mutant larvae shifted to restrictive temperature, and feeding ecd-1 larvae 20-hydroxyecdysone triggered abortive pupariation, demonstrating that the ecd-1 mutation acts upstream of ecdysone synthesis or secretion.","method":"HPLC ecdysteroid analysis, radioimmunoassay, hormone feeding rescue experiments, developmental staging","journal":"General and Comparative Endocrinology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — biochemical measurement of ecdysteroids combined with hormone rescue, establishing epistatic relationship between ecd locus and ecdysone production","pmids":["6427061"],"is_preprint":false}],"current_model":"ECD (ecdysoneless homolog) is an evolutionarily conserved protein that functions as a chaperone for Prp8/U5 snRNP biogenesis in the cytoplasm (required for pre-mRNA splicing fidelity), interacts with the R2TP cochaperone complex (via RUVBL1 and CK2-phosphorylation-dependent PIH1D1 binding) to regulate cell cycle progression, acts as a negative regulator of the PERK arm of the unfolded protein response by stabilizing GRP78 protein and coimmunoprecipitating with PERK, and in cancer contexts promotes invasion/metastasis by competitively shielding hnRNP F from ZFP91-mediated ubiquitination/degradation and by acting downstream of an ACK1-AKT-POU2F1 transcriptional axis to facilitate p53 ubiquitination."},"narrative":{"mechanistic_narrative":"ECD (ecdysoneless homolog) is an evolutionarily conserved cofactor that links pre-mRNA splicing machinery biogenesis to cell-cycle progression and stress survival, with prominent oncogenic activity when overexpressed [PMID:33444449, PMID:26711270]. In the cytoplasm, ECD acts as a chaperone for U5 snRNP assembly: it delivers and stabilizes the Prp8 protein, and its loss collapses Prp8 levels and U5 snRNP biogenesis, degrading splicing fidelity [PMID:33444449]. ECD couples to the R2TP cochaperone complex, binding RUVBL1 in a phosphorylation-independent manner that is the key determinant for its cell-cycle function, while CK2-mediated phosphorylation drives a secondary, dispensable interaction with PIH1D1 [PMID:26711270]. ECD also restrains the PERK arm of the unfolded protein response by post-translationally stabilizing GRP78, thereby lowering phospho-PERK, phospho-eIF2α, and ATF4 and conferring a survival advantage under ER stress [PMID:28652267]. In gastric cancer, ECD is transcriptionally induced through an ACK1–AKT–POU2F1 axis, with POU2F1 binding the ECD promoter, and it then acts as an effector that promotes EMT, migration, and invasion [PMID:25678401]; mechanistically it shields hnRNP F from ZFP91-mediated ubiquitination via its N-terminal STG1 domain [PMID:29706618] and promotes ubiquitination and degradation of the tumor suppressor p53 downstream of ACK1 [PMID:26498357]. The founding Drosophila genetics established ecd as essential for development, molting, eclosion, and fertility, acting upstream of ecdysteroid production [PMID:8293578, PMID:6427061].","teleology":[{"year":1984,"claim":"Established the founding phenotype linking the ecd locus to hormone-dependent development, showing it acts upstream of ecdysone synthesis or secretion.","evidence":"temperature-sensitive Drosophila mutant with HPLC/RIA ecdysteroid measurement and 20-hydroxyecdysone feeding rescue","pmids":["6427061"],"confidence":"Medium","gaps":["No molecular function for the gene product identified","Mechanism by which ecd influences ecdysteroid levels unknown"]},{"year":1993,"claim":"Defined ecd as an essential developmental gene with both prezygotic and postzygotic roles across the life cycle, beyond the single hormone phenotype.","evidence":"Drosophila gene dosage, complementation, and allelic-series phenotyping","pmids":["8293578"],"confidence":"Medium","gaps":["No biochemical activity assigned","Does not connect developmental requirement to a molecular pathway"]},{"year":2015,"claim":"Resolved how ECD engages the R2TP cochaperone complex and which contact drives its cell-cycle function, distinguishing the essential RUVBL1 interaction from a dispensable CK2/PIH1D1-dependent one.","evidence":"reciprocal Co-IP, in vitro binding with phospho-deficient mutants, and rescue of Ecd-KO cells","pmids":["26711270"],"confidence":"High","gaps":["Direct cell-cycle substrates or clients of the ECD–R2TP module not defined","Structural basis of RUVBL1 binding unresolved"]},{"year":2015,"claim":"Placed ECD as a transcriptionally regulated effector of an upstream oncogenic kinase axis driving invasion.","evidence":"SILAC proteomics, POU2F1 ChIP on the ECD promoter, siRNA epistasis, and in vivo metastasis in gastric cancer models","pmids":["25678401"],"confidence":"High","gaps":["Molecular effectors of ECD's EMT-promoting activity not defined in this study","Generality beyond gastric cancer not addressed"]},{"year":2017,"claim":"Identified ECD as a negative regulator of PERK-arm UPR signaling acting through post-translational stabilization of GRP78.","evidence":"reciprocal Co-IP, gain/loss-of-function with pathway immunoblots, and GRP78-knockdown epistasis","pmids":["28652267"],"confidence":"High","gaps":["Mechanism by which ECD stabilizes GRP78 protein not defined","Whether this links to ECD's chaperone/R2TP roles unknown"]},{"year":2017,"claim":"Connected ECD to tumor-suppressor control by showing it promotes p53 ubiquitination and degradation downstream of ACK1.","evidence":"ubiquitination assays, siRNA/overexpression epistasis, colony formation and cell-cycle assays","pmids":["26498357"],"confidence":"Medium","gaps":["E3/E2 machinery ECD uses for p53 ubiquitination not identified","Single-lab finding without independent confirmation"]},{"year":2018,"claim":"Defined a direct molecular mechanism for ECD's pro-metastatic activity: competitive protection of a substrate from an E3 ligase.","evidence":"Co-IP with truncation domain mapping, ubiquitination assays, invasion/migration assays, and in vivo metastasis","pmids":["29706618"],"confidence":"High","gaps":["Whether STG1-domain shielding extends to other substrates unknown","Structural detail of the ECD–hnRNP F interface unresolved"]},{"year":2021,"claim":"Established the conserved core molecular function of ECD as a cytoplasmic chaperone for Prp8 and U5 snRNP biogenesis required for splicing fidelity.","evidence":"Drosophila genetic loss-of-function with splicing readouts and Co-IP/MS partner identification (SmD3)","pmids":["33444449"],"confidence":"High","gaps":["Mechanism of Prp8 delivery to nascent U5 snRNPs not defined at structural level","Whether splicing role explains mammalian cell-cycle and cancer phenotypes not tested"]},{"year":null,"claim":"How ECD's conserved splicing/chaperone function mechanistically integrates with its R2TP cell-cycle role, UPR regulation, and substrate-shielding oncogenic activities remains unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No unifying biochemical model linking the splicing, cell-cycle, UPR, and ubiquitination functions","Direct enzymatic activity of ECD remains undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0044183","term_label":"protein folding chaperone","supporting_discovery_ids":[0]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[1,2,3]},{"term_id":"GO:0140313","term_label":"molecular sequestering activity","supporting_discovery_ids":[3]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[0]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[1]},{"term_id":"R-HSA-8953897","term_label":"Cellular responses to stimuli","supporting_discovery_ids":[2]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[3,4,5]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[6,7]}],"complexes":["R2TP cochaperone complex","U5 snRNP"],"partners":["PRPF8","SNRPD3","RUVBL1","PIH1D1","EIF2AK3","HSPA5","HNRNPF"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O95905","full_name":"Protein ecdysoneless homolog","aliases":["Human suppressor of GCR two","hSGT1"],"length_aa":644,"mass_kda":72.8,"function":"Regulator of p53/TP53 stability and function. Inhibits MDM2-mediated degradation of p53/TP53 possibly by cooperating in part with TXNIP (PubMed:16849563, PubMed:23880345). May be involved transcriptional regulation. In vitro has intrinsic transactivation activity enhanced by EP300. May be a transcriptional activator required for the expression of glycolytic genes (PubMed:19919181, PubMed:9928932). Involved in regulation of cell cycle progression. Proposed to disrupt Rb-E2F binding leading to transcriptional activation of E2F proteins (PubMed:19640839). The cell cycle -regulating function may depend on its RUVBL1-mediated association with the R2TP complex (PubMed:26711270). May play a role in regulation of pre-mRNA splicing (PubMed:24722212). Participates together with DDX39A in mRNA nuclear export (PubMed:33941617)","subcellular_location":"Cytoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/O95905/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/ECD","classification":"Common Essential","n_dependent_lines":1207,"n_total_lines":1208,"dependency_fraction":0.9991721854304636},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"DNAJC7","stoichiometry":0.2},{"gene":"EFTUD2","stoichiometry":0.2},{"gene":"MYO1B","stoichiometry":0.2},{"gene":"MYO9B","stoichiometry":0.2},{"gene":"PRPF8","stoichiometry":0.2},{"gene":"PTGES3","stoichiometry":0.2},{"gene":"SNRPD2","stoichiometry":0.2},{"gene":"SNRPF","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/ECD","total_profiled":1310},"omim":[{"mim_id":"619906","title":"DExD-BOX HELICASE 39A; DDX39A","url":"https://www.omim.org/entry/619906"},{"mim_id":"619671","title":"ALK AND LTK LIGAND 2; ALKAL2","url":"https://www.omim.org/entry/619671"},{"mim_id":"619670","title":"ALK AND LTK LIGAND 1; ALKAL1","url":"https://www.omim.org/entry/619670"},{"mim_id":"619495","title":"ADAM METALLOPEPTIDASE DOMAIN-CONTAINING PROTEIN 18; ADAM18","url":"https://www.omim.org/entry/619495"},{"mim_id":"616464","title":"ECDYSONELESS CELL CYCLE REGULATOR; ECD","url":"https://www.omim.org/entry/616464"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Cytosol","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ECD"},"hgnc":{"alias_symbol":["hSGT1","GCR2"],"prev_symbol":[]},"alphafold":{"accession":"O95905","domains":[{"cath_id":"-","chopping":"14-153_161-196","consensus_level":"high","plddt":90.568,"start":14,"end":196},{"cath_id":"1.10.1220","chopping":"207-315","consensus_level":"high","plddt":92.9073,"start":207,"end":315}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O95905","model_url":"https://alphafold.ebi.ac.uk/files/AF-O95905-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O95905-F1-predicted_aligned_error_v6.png","plddt_mean":76.0},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ECD","jax_strain_url":"https://www.jax.org/strain/search?query=ECD"},"sequence":{"accession":"O95905","fasta_url":"https://rest.uniprot.org/uniprotkb/O95905.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O95905/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O95905"}},"corpus_meta":[{"pmid":"17090006","id":"PMC_17090006","title":"Top-down 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inhibition of ADAM metalloproteases blocks HER-2 extracellular domain (ECD) cleavage and potentiates the anti-tumor effects of trastuzumab.","date":"2006","source":"Cancer biology & therapy","url":"https://pubmed.ncbi.nlm.nih.gov/16627988","citation_count":53,"is_preprint":false},{"pmid":"10486149","id":"PMC_10486149","title":"Jararhagin ECD-containing disintegrin domain: expression in escherichia coli and inhibition of the platelet-collagen interaction.","date":"1999","source":"Archives of biochemistry and biophysics","url":"https://pubmed.ncbi.nlm.nih.gov/10486149","citation_count":52,"is_preprint":false},{"pmid":"18400512","id":"PMC_18400512","title":"Probing the gas-phase folding kinetics of peptide ions by IR activated DR-ECD.","date":"2008","source":"Journal of the American Society for Mass Spectrometry","url":"https://pubmed.ncbi.nlm.nih.gov/18400512","citation_count":47,"is_preprint":false},{"pmid":"31816682","id":"PMC_31816682","title":"Quantum dots as nanolabels for breast 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American Society for Mass Spectrometry","url":"https://pubmed.ncbi.nlm.nih.gov/24781457","citation_count":10,"is_preprint":false},{"pmid":"17962038","id":"PMC_17962038","title":"Identification of single and double sites of phosphorylation by ECD FT-ICR/MS in peptides related to the phosphorylation site domain of the myristoylated alanine-rich C kinase protein.","date":"2007","source":"Journal of the American Society for Mass Spectrometry","url":"https://pubmed.ncbi.nlm.nih.gov/17962038","citation_count":10,"is_preprint":false},{"pmid":"26162650","id":"PMC_26162650","title":"HDX match software for the data analysis of top-down ECD-FTMS hydrogen/deuterium exchange experiments.","date":"2015","source":"Journal of the American Society for Mass Spectrometry","url":"https://pubmed.ncbi.nlm.nih.gov/26162650","citation_count":10,"is_preprint":false},{"pmid":"26421831","id":"PMC_26421831","title":"Decreased regional cerebral blood flow in the bilateral thalami and medulla oblongata determined by an easy Z-score (eZIS) analysis of (99m)Tc-ECD-SPECT images in a case of MM2-thalamic-type sporadic Creutzfeldt-Jakob disease.","date":"2015","source":"Journal of the neurological sciences","url":"https://pubmed.ncbi.nlm.nih.gov/26421831","citation_count":10,"is_preprint":false},{"pmid":"7725799","id":"PMC_7725799","title":"A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8 new open reading frames of unknown function.","date":"1994","source":"Yeast (Chichester, England)","url":"https://pubmed.ncbi.nlm.nih.gov/7725799","citation_count":9,"is_preprint":false},{"pmid":"22339939","id":"PMC_22339939","title":"Relationships between serum HER2 ECD, TIMP-1 and clinical outcomes in Taiwanese breast cancer.","date":"2012","source":"World journal of surgical oncology","url":"https://pubmed.ncbi.nlm.nih.gov/22339939","citation_count":9,"is_preprint":false},{"pmid":"11971215","id":"PMC_11971215","title":"Significance of 99mTc-ECD SPECT in acute and subacute ischemic stroke: comparison with MR images including diffusion and perfusion weighted images.","date":"2002","source":"Yonsei medical journal","url":"https://pubmed.ncbi.nlm.nih.gov/11971215","citation_count":9,"is_preprint":false},{"pmid":"24289611","id":"PMC_24289611","title":"In silico design of discontinuous peptides representative of B and T-cell epitopes from HER2-ECD as potential novel cancer peptide vaccines.","date":"2013","source":"Asian Pacific journal of cancer prevention : APJCP","url":"https://pubmed.ncbi.nlm.nih.gov/24289611","citation_count":9,"is_preprint":false},{"pmid":"25089226","id":"PMC_25089226","title":"Interference-Free HER2 ECD as a Serum Biomarker in Breast Cancer.","date":"2014","source":"Journal of molecular biomarkers & diagnosis","url":"https://pubmed.ncbi.nlm.nih.gov/25089226","citation_count":9,"is_preprint":false},{"pmid":"8072744","id":"PMC_8072744","title":"A comparative study of 99Tcm-HMPAO and 99Tcm-ECD as a leukocyte labelling agent.","date":"1994","source":"Nuclear medicine communications","url":"https://pubmed.ncbi.nlm.nih.gov/8072744","citation_count":9,"is_preprint":false},{"pmid":"28856210","id":"PMC_28856210","title":"Development and implementation of an HPLC-ECD method for analysis of vitamin C in plasma using single column and automatic alternating dual column regeneration.","date":"2016","source":"Practical laboratory medicine","url":"https://pubmed.ncbi.nlm.nih.gov/28856210","citation_count":9,"is_preprint":false},{"pmid":"11577763","id":"PMC_11577763","title":"Interictal crossed cerebellar hyperperfusion on Tc-99m ECD SPECT.","date":"2001","source":"Annals of nuclear medicine","url":"https://pubmed.ncbi.nlm.nih.gov/11577763","citation_count":9,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":49643,"output_tokens":3245,"usd":0.098802,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":9753,"output_tokens":2968,"usd":0.061483,"stage2_stop_reason":"end_turn"},"total_usd":0.160285,"stage1_batch_id":"msgbatch_01AsR7g8dGTEiEw9U83bJeWn","stage2_batch_id":"msgbatch_01YV5ZyxtFNUZEjxRcpd9jzb","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking through the abstracts, I need to identify papers about the canonical ECD gene (human ecdysoneless homolog, also known as hSGT1/GCR2 in certain contexts). Let me classify each paper:\n\n- Papers about ECD as \"electron capture dissociation\" (MS technique): EXCLUDE\n- Papers about HER2 ECD (extracellular domain): EXCLUDE  \n- Papers about Notch3 ECD (extracellular domain): EXCLUDE\n- Papers about Erdheim-Chester Disease (ECD): EXCLUDE\n- Papers about GCR2 in yeast (Saccharomyces cerevisiae) as Gcr2p transcription factor: This is a yeast protein involved in glycolytic gene activation - need to assess if ortholog\n- Papers about the Drosophila ecdysoneless (ecd) gene: INCLUDE as ortholog\n- Papers about mammalian ECD (ecdysoneless homolog): INCLUDE\n\nKey papers about the canonical ECD protein:\n- PMID 25678401: ACK1-AKT-POU2F1-ECD signaling in gastric cancer\n- PMID 29706618: ECD protects hnRNP F from ubiquitination by ZFP91\n- PMID 26498357: ECD-dependent p53 ubiquitination\n- PMID 26711270: ECD interaction with RUVBL1 and R2TP complex\n- PMID 28652267: ECD as negative regulator of PERK arm of UPR\n- PMID 33444449: Ecd promotes U5 snRNP maturation and Prp8 stability\n- PMID 8293578: Drosophila ecd developmental requirements\n- PMID 6427061: Drosophila l(3)ecd-1ts ecdysteroid deficit\n- PMID 1508187: Yeast GCR2 - transcriptional activation of glycolytic genes\n- PMID 7713414: GCR1/GCR2 interaction\n- PMID 10606743: Sgc1p suppressor of gcr2\n- PMID 15617685: Reverse recruitment via Nup84/Gcr2\n\nFor yeast GCR2: The human ECD gene alias \"GCR2\" refers to the human ecdysoneless protein, not the yeast Gcr2p. The yeast Gcr2p is a transcriptional activator of glycolytic genes - this is a fundamentally different function from the mammalian ECD protein. This appears to be a symbol collision/alias issue. I'll exclude yeast GCR2 papers as the alias \"GCR2\" for the human ECD gene likely refers to a different historical naming, not the yeast glycolytic regulator.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"Drosophila Ecdysoneless (Ecd) promotes U5 snRNP assembly and stabilizes Prp8 protein. Ecd delivers Prp8 to the emerging U5 snRNPs in the cytoplasm; Ecd deficiency leads to reduced Prp8 protein levels and compromised U5 snRNP biogenesis, causing loss of splicing fidelity. SmD3 was identified as a novel interaction partner of Ecd by proteomic approaches.\",\n      \"method\": \"Drosophila genetics, proteomic approaches (Co-IP/MS), loss-of-function with splicing fidelity readout\",\n      \"journal\": \"Nucleic Acids Research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — Drosophila genetic loss-of-function combined with proteomic identification of interaction partners and defined molecular phenotype (Prp8 destabilization, U5 snRNP biogenesis failure, splicing defects), multiple orthogonal methods in single study\",\n      \"pmids\": [\"33444449\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Mammalian ECD interacts with the R2TP cochaperone complex component RUVBL1 in a phosphorylation-independent manner, and this interaction is essential for ECD's cell cycle progression function. ECD also undergoes CK2-mediated phosphorylation that facilitates interaction with PIH1D1 (another R2TP component), but phosphorylation-deficient ECD mutants that lose PIH1D1 binding still interact with R2TP and partially retain cell cycle function. The RUVBL1 interaction is the key functional determinant for rescuing Ecd-deficient cells from cell cycle arrest.\",\n      \"method\": \"Biochemical Co-IP, in vitro binding assays with phosphorylation-deficient mutants, rescue of Ecd-KO cells with mutant constructs\",\n      \"journal\": \"Molecular and Cellular Biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal biochemical interaction mapping with mutagenesis, functional rescue assays in Ecd-deficient cells, two orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"26711270\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Mammalian ECD is a negative regulator of the PERK arm of the unfolded protein response (UPR). ECD colocalizes and coimmunoprecipitates with PERK and GRP78. ECD depletion increases phospho-PERK and phospho-eIF2α levels; ECD overexpression decreases p-PERK, p-eIF2α, and ATF4 but increases GRP78 protein (without increasing GRP78 mRNA, suggesting posttranslational regulation). Knockdown of GRP78 reverses ECD's attenuation of PERK signaling. ECD overexpression confers survival advantage under ER stress.\",\n      \"method\": \"Co-immunoprecipitation, colocalization, siRNA knockdown, overexpression, immunoblot for pathway components, GRP78 knockdown epistasis\",\n      \"journal\": \"Molecular and Cellular Biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP, epistasis (GRP78 KD reversal), loss- and gain-of-function with defined pathway readouts, multiple orthogonal methods in single study\",\n      \"pmids\": [\"28652267\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"ECD promotes gastric cancer invasion and metastasis by protecting hnRNP F from ubiquitination and proteasomal degradation. ZFP91 was identified as the E3 ubiquitin ligase responsible for hnRNP F ubiquitination at Lys185. ECD competitively binds hnRNP F via its N-terminal STG1 domain (residues 13–383), preventing hnRNP F from interacting with ZFP91, thus blocking ZFP91-mediated ubiquitination and degradation of hnRNP F.\",\n      \"method\": \"Co-IP, domain mapping with truncation mutants, ubiquitination assay, proteasome inhibitor experiments, siRNA knockdown, in vitro invasion/migration assays, in vivo metastasis model\",\n      \"journal\": \"Cell Death & Disease\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP with domain mapping, in vitro ubiquitination assay, functional rescue/epistasis with defined molecular mechanism, multiple orthogonal methods\",\n      \"pmids\": [\"29706618\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"In gastric cancer, ACK1 activates AKT (phosphorylation at Thr308 and Ser473), which upregulates the transcription factor POU2F1; POU2F1 directly binds the promoter of ECD and transcriptionally activates ECD expression. ECD overexpression downstream of this pathway promotes EMT, migration, and invasion. Silencing ECD completely blocks ACK1-overexpression-induced EMT, migration, and invasion, placing ECD as a functional effector in the ACK1-AKT-POU2F1-ECD signaling axis.\",\n      \"method\": \"SILAC quantitative proteomics, siRNA knockdown, chromatin immunoprecipitation (POU2F1 on ECD promoter), overexpression, in vitro migration/invasion, in vivo metastasis\",\n      \"journal\": \"The Journal of Pathology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — SILAC proteomics, ChIP validation of promoter binding, genetic epistasis by siRNA, multiple orthogonal methods in single study\",\n      \"pmids\": [\"25678401\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"ECD promotes gastric cancer tumorigenesis via ubiquitination and degradation of the tumor suppressor p53. Overexpression of ECD or ACK1 promotes p53 ubiquitination and decreases p53 levels; silencing of ECD decreases p53 ubiquitination and increases p53 levels. Silencing ECD attenuates the enhancement of p53 ubiquitination induced by ACK1 overexpression, placing ECD downstream of ACK1 in controlling p53 stability.\",\n      \"method\": \"Ubiquitination assay, siRNA knockdown, overexpression, immunoblot, colony formation and cell cycle assays\",\n      \"journal\": \"Oncotarget\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — ubiquitination assay and epistasis experiments, but single lab and the direct E3/E2 machinery used by ECD for p53 ubiquitination was not identified in this study\",\n      \"pmids\": [\"26498357\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1993,\n      \"finding\": \"The Drosophila ecdysoneless (ecd) locus is required for embryonic development, successful completion of each larval molt, adult eclosion, and female fertility. Mutant allele analysis showed ecd is required for normal macrochaete differentiation. Gene dosage and complementation studies with five nonconditional lethal alleles established that ecd plays both prezygotic and postzygotic roles essential for normal development. Severity of phenotype correlated with ecd mutant genotype.\",\n      \"method\": \"Drosophila genetics — gene dosage, complementation tests, phenotypic analysis of multiple alleles\",\n      \"journal\": \"Developmental Genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — systematic genetic analysis with multiple alleles across developmental stages, single lab but comprehensive allelic series\",\n      \"pmids\": [\"8293578\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1984,\n      \"finding\": \"The Drosophila temperature-sensitive l(3)ecd-1ts mutation causes an ecdysteroid deficit at the restrictive temperature (29°C), blocking pupariation. HPLC and RIA analyses confirmed low ecdysteroid levels in mutant larvae shifted to restrictive temperature, and feeding ecd-1 larvae 20-hydroxyecdysone triggered abortive pupariation, demonstrating that the ecd-1 mutation acts upstream of ecdysone synthesis or secretion.\",\n      \"method\": \"HPLC ecdysteroid analysis, radioimmunoassay, hormone feeding rescue experiments, developmental staging\",\n      \"journal\": \"General and Comparative Endocrinology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — biochemical measurement of ecdysteroids combined with hormone rescue, establishing epistatic relationship between ecd locus and ecdysone production\",\n      \"pmids\": [\"6427061\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ECD (ecdysoneless homolog) is an evolutionarily conserved protein that functions as a chaperone for Prp8/U5 snRNP biogenesis in the cytoplasm (required for pre-mRNA splicing fidelity), interacts with the R2TP cochaperone complex (via RUVBL1 and CK2-phosphorylation-dependent PIH1D1 binding) to regulate cell cycle progression, acts as a negative regulator of the PERK arm of the unfolded protein response by stabilizing GRP78 protein and coimmunoprecipitating with PERK, and in cancer contexts promotes invasion/metastasis by competitively shielding hnRNP F from ZFP91-mediated ubiquitination/degradation and by acting downstream of an ACK1-AKT-POU2F1 transcriptional axis to facilitate p53 ubiquitination.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ECD (ecdysoneless homolog) is an evolutionarily conserved cofactor that links pre-mRNA splicing machinery biogenesis to cell-cycle progression and stress survival, with prominent oncogenic activity when overexpressed [#0, #1]. In the cytoplasm, ECD acts as a chaperone for U5 snRNP assembly: it delivers and stabilizes the Prp8 protein, and its loss collapses Prp8 levels and U5 snRNP biogenesis, degrading splicing fidelity [#0]. ECD couples to the R2TP cochaperone complex, binding RUVBL1 in a phosphorylation-independent manner that is the key determinant for its cell-cycle function, while CK2-mediated phosphorylation drives a secondary, dispensable interaction with PIH1D1 [#1]. ECD also restrains the PERK arm of the unfolded protein response by post-translationally stabilizing GRP78, thereby lowering phospho-PERK, phospho-eIF2\\u03b1, and ATF4 and conferring a survival advantage under ER stress [#2]. In gastric cancer, ECD is transcriptionally induced through an ACK1\\u2013AKT\\u2013POU2F1 axis, with POU2F1 binding the ECD promoter, and it then acts as an effector that promotes EMT, migration, and invasion [#4]; mechanistically it shields hnRNP F from ZFP91-mediated ubiquitination via its N-terminal STG1 domain [#3] and promotes ubiquitination and degradation of the tumor suppressor p53 downstream of ACK1 [#5]. The founding Drosophila genetics established ecd as essential for development, molting, eclosion, and fertility, acting upstream of ecdysteroid production [#6, #7].\",\n  \"teleology\": [\n    {\n      \"year\": 1984,\n      \"claim\": \"Established the founding phenotype linking the ecd locus to hormone-dependent development, showing it acts upstream of ecdysone synthesis or secretion.\",\n      \"evidence\": \"temperature-sensitive Drosophila mutant with HPLC/RIA ecdysteroid measurement and 20-hydroxyecdysone feeding rescue\",\n      \"pmids\": [\"6427061\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No molecular function for the gene product identified\", \"Mechanism by which ecd influences ecdysteroid levels unknown\"]\n    },\n    {\n      \"year\": 1993,\n      \"claim\": \"Defined ecd as an essential developmental gene with both prezygotic and postzygotic roles across the life cycle, beyond the single hormone phenotype.\",\n      \"evidence\": \"Drosophila gene dosage, complementation, and allelic-series phenotyping\",\n      \"pmids\": [\"8293578\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No biochemical activity assigned\", \"Does not connect developmental requirement to a molecular pathway\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Resolved how ECD engages the R2TP cochaperone complex and which contact drives its cell-cycle function, distinguishing the essential RUVBL1 interaction from a dispensable CK2/PIH1D1-dependent one.\",\n      \"evidence\": \"reciprocal Co-IP, in vitro binding with phospho-deficient mutants, and rescue of Ecd-KO cells\",\n      \"pmids\": [\"26711270\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct cell-cycle substrates or clients of the ECD\\u2013R2TP module not defined\", \"Structural basis of RUVBL1 binding unresolved\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Placed ECD as a transcriptionally regulated effector of an upstream oncogenic kinase axis driving invasion.\",\n      \"evidence\": \"SILAC proteomics, POU2F1 ChIP on the ECD promoter, siRNA epistasis, and in vivo metastasis in gastric cancer models\",\n      \"pmids\": [\"25678401\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular effectors of ECD's EMT-promoting activity not defined in this study\", \"Generality beyond gastric cancer not addressed\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Identified ECD as a negative regulator of PERK-arm UPR signaling acting through post-translational stabilization of GRP78.\",\n      \"evidence\": \"reciprocal Co-IP, gain/loss-of-function with pathway immunoblots, and GRP78-knockdown epistasis\",\n      \"pmids\": [\"28652267\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism by which ECD stabilizes GRP78 protein not defined\", \"Whether this links to ECD's chaperone/R2TP roles unknown\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Connected ECD to tumor-suppressor control by showing it promotes p53 ubiquitination and degradation downstream of ACK1.\",\n      \"evidence\": \"ubiquitination assays, siRNA/overexpression epistasis, colony formation and cell-cycle assays\",\n      \"pmids\": [\"26498357\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"E3/E2 machinery ECD uses for p53 ubiquitination not identified\", \"Single-lab finding without independent confirmation\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Defined a direct molecular mechanism for ECD's pro-metastatic activity: competitive protection of a substrate from an E3 ligase.\",\n      \"evidence\": \"Co-IP with truncation domain mapping, ubiquitination assays, invasion/migration assays, and in vivo metastasis\",\n      \"pmids\": [\"29706618\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether STG1-domain shielding extends to other substrates unknown\", \"Structural detail of the ECD\\u2013hnRNP F interface unresolved\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Established the conserved core molecular function of ECD as a cytoplasmic chaperone for Prp8 and U5 snRNP biogenesis required for splicing fidelity.\",\n      \"evidence\": \"Drosophila genetic loss-of-function with splicing readouts and Co-IP/MS partner identification (SmD3)\",\n      \"pmids\": [\"33444449\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism of Prp8 delivery to nascent U5 snRNPs not defined at structural level\", \"Whether splicing role explains mammalian cell-cycle and cancer phenotypes not tested\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How ECD's conserved splicing/chaperone function mechanistically integrates with its R2TP cell-cycle role, UPR regulation, and substrate-shielding oncogenic activities remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No unifying biochemical model linking the splicing, cell-cycle, UPR, and ubiquitination functions\", \"Direct enzymatic activity of ECD remains undefined\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0044183\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [1, 2, 3]},\n      {\"term_id\": \"GO:0140313\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-8953897\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [3, 4, 5]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [6, 7]}\n    ],\n    \"complexes\": [\"R2TP cochaperone complex\", \"U5 snRNP\"],\n    \"partners\": [\"PRPF8\", \"SNRPD3\", \"RUVBL1\", \"PIH1D1\", \"EIF2AK3\", \"HSPA5\", \"HNRNPF\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}