{"gene":"LSM14B","run_date":"2026-06-10T02:59:50","timeline":{"discoveries":[{"year":2004,"finding":"LSM14B (Lsm13/RAP55B) was identified as a novel Lsm domain protein with a long C-terminal tail, containing an N-terminal Lsm domain predicted to bind nucleic acids; computational analysis suggested involvement in regulation of the mitotic G2/M phase based on known yeast interaction partners.","method":"Integrative bioinformatics / computational domain analysis","journal":"FEBS letters","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational prediction only, no experimental validation of binding or function","pmids":["15225602"],"is_preprint":false},{"year":2008,"finding":"RAP55B (LSM14B) shares multiple conserved domains with RAP55A including the LSm14 domain, serine/threonine-rich region, FDF motif, FFD-TFG box, and RGG repeats; Xenopus RAP55B (xRAP55B) was shown to be part of translationally repressed mRNP complexes in early oocytes.","method":"Sequence analysis and biochemical characterization of mRNP complexes in Xenopus oocytes","journal":"The international journal of biochemistry & cell biology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — domain characterization and mRNP association reported in a review/analysis paper with limited experimental detail in abstract","pmids":["18723115"],"is_preprint":false},{"year":2010,"finding":"RAP55B (LSM14B) was identified as a component of the CPEB RNP complex in Xenopus oocytes, interacting with CPEB, Xp54, eIF4E1b, and ePAB; epitope-tagged xPat1 proteins co-immunoprecipitated RAP55B from oocyte extracts.","method":"Co-immunoprecipitation of epitope-tagged Pat1 proteins from Xenopus oocyte extracts","journal":"RNA (New York, N.Y.)","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — Co-IP from oocyte extracts with multiple interaction partners identified; single lab but confirmed in a broader complex context","pmids":["20826699"],"is_preprint":false},{"year":2012,"finding":"RAP55B (LSM14B) localizes to processing bodies (P-bodies) when expressed in human cultured cells; high-level expression of RAP55B induces formation of SG-like large cytoplasmic mRNP granules that contain both P-body and stress granule components.","method":"Fluorescence microscopy of expressed RAP55B in human cultured cells; immunostaining for P-body and SG markers","journal":"RNA biology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization experiment with functional consequence (granule assembly), single lab, two orthogonal readouts","pmids":["22614839"],"is_preprint":false},{"year":2015,"finding":"Xenopus RAPB (xRAPB, LSM14B ortholog) specifically interacts with the DDX6 helicase Xp54; unlike xRAPA, xRAPB is detected in polysomes and stalled translation initiation complexes and its overexpression leads to selective binding to translatable mRNA species without causing translation repression or mRNA degradation, suggesting a role in mRNA translational activation rather than repression.","method":"Co-immunoprecipitation, polysome fractionation, RNA binding assays in Xenopus oocytes","journal":"Biochimica et biophysica acta","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal biochemical evidence (Co-IP, polysome profiling) in a single lab with multiple orthogonal methods","pmids":["26455898"],"is_preprint":false},{"year":2017,"finding":"LSM14B is essential for oocyte meiotic maturation in mice; knockdown/loss of LSM14B causes meiotic arrest at metaphase, chromosome misalignment, and abnormal spindle assembly checkpoint (SAC) and maturation promoting factor (MPF) activation; Cyclin B1 and Cdc20 mRNAs were identified as likely direct targets whose levels changed with LSM14B expression.","method":"LSM14B knockdown in mouse oocytes; immunofluorescence for spindle and chromosome organization; mRNA level analysis","journal":"The Journal of reproduction and development","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function with defined cellular phenotype and identification of mRNA targets; single lab","pmids":["28458300"],"is_preprint":false},{"year":2023,"finding":"LSM14B is an oocyte-specific RNA-binding protein that acts as an interaction hub for proteins and mRNAs throughout oocyte development; deletion of Lsm14b causes female-specific infertility with oocytes unable to complete meiosis or support early embryogenesis; LSM14B regulates translation of a subset of its bound mRNAs; RNP complexes tethered by LSM14B are exclusive to oocytes.","method":"mRNA-interactome capture to identify oocyte RBPs; Lsm14b knockout mouse model; translation reporter assays; proteomic interaction studies","journal":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic knockout with defined infertility phenotype, mRNA-interactome capture, proteomic interaction mapping; multiple orthogonal methods in a single comprehensive study","pmids":["37083226"],"is_preprint":false},{"year":2023,"finding":"LSM14B is a component of membraneless compartments including P-body-like granules and mitochondria-associated ribonucleoprotein domains (MARDO) in germ cells; loss of LSM14B disrupts primordial follicle assembly, impairs maternal mRNA accumulation and stability in non-growing oocytes (concomitant with impaired P-body-like granule assembly), and disrupts translation in fully grown oocytes associated with dissolution of MARDO components; Lsm14b-deficient oocytes show compromised maturation promoting factor activation that can be rescued by WEE1/2 inhibitor.","method":"Lsm14b conditional knockout mouse; 10x Genomics single-cell RNA-seq; RNA-seq of GV-stage oocytes; immunostaining for P-body and MARDO components; WEE1/2 inhibitor rescue experiment","journal":"Cellular and molecular life sciences : CMLS","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic knockout with multiple orthogonal methods (scRNA-seq, bulk RNA-seq, immunostaining, pharmacological rescue), single lab but comprehensive","pmids":["37578641"],"is_preprint":false},{"year":2023,"finding":"LSM14B regulates oocyte maturation through control of P-body function; loss of LSM14B in mouse ovaries causes aberrant transcriptional activation (altered non-surrounded nucleolus/surrounded nucleolus oocyte proportions), abnormal chromosome assembly and segregation, and changes in expression/localization of P-body components LSM14A, DCP1A, and 4E-T; DDX6 is downregulated and abnormally accumulates in the nucleus in Lsm14b-deficient oocytes.","method":"Lsm14b knockout mouse; global transcriptome analysis; immunostaining for P-body components; nuclear/cytoplasmic localization analysis of DDX6","journal":"Journal of genetics and genomics = Yi chuan xue bao","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic knockout with transcriptome analysis and immunostaining for specific pathway components; multiple orthogonal methods","pmids":["37481122"],"is_preprint":false},{"year":2024,"finding":"A complex of DDX6, LSM14B, and CPEB1 directly represses cyclin B1 translation in mouse oocytes through interaction with the cyclin B1 3'UTR, thereby maintaining prophase arrest; this was demonstrated using Trim-Away protein depletion of each component.","method":"Trim-Away depletion of DDX6, LSM14B, and CPEB1 in mouse oocytes; translational reporter assay for cyclin B1; RNA interaction assay with 3'UTR","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — Trim-Away protein depletion with translational reporter and defined 3'UTR interaction; multiple proteins tested with phenotypic rescue; published in high-quality journal","pmids":["39567493"],"is_preprint":false},{"year":2024,"finding":"LSM14B knockdown in oocytes from normal-diet mice recapitulates translation defects, mitochondrial dysfunction, and meiotic defects seen in obese mice; injection of Lsm14b mRNA into oocytes from high-fat diet mice rescues these phenotypes, establishing that LSM14B mediates maternal mRNA storage and translation required for oocyte quality.","method":"siRNA knockdown and mRNA rescue injection in mouse oocytes; RNA-seq; functional assays for mitochondrial function and meiotic progression","journal":"Free radical biology & medicine","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function and gain-of-function rescue experiment with defined phenotypic readouts; single lab","pmids":["38552928"],"is_preprint":false},{"year":2025,"finding":"LSM14B physically associates with Musashi1 through its N-terminal RNA recognition motifs (not the C-terminal domain used by other Musashi partners) and is required for Musashi1-dependent translational activation of target mRNAs during Xenopus oocyte maturation; LSM14B also mediates Musashi1-dependent translational activation of the mammalian Prop1 mRNA.","method":"Co-immunoprecipitation; domain mapping by mutagenesis; translational reporter assays in Xenopus oocytes; rescue experiments","journal":"Scientific reports","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP with domain mapping, functional rescue assay, and mammalian mRNA target validation; multiple orthogonal methods in one study","pmids":["40211036"],"is_preprint":false},{"year":2025,"finding":"LSM14B acts as a negative regulator of P-body formation in somatic epithelial cells; glucocorticoid treatment decreases LSM14B levels and this decrease is linked to P-body accumulation and sequestration of AU-rich mRNAs, reducing their translation yield.","method":"Genetic invalidation and rescue of LSM14B; FDA-approved drug screen; fluorescence microscopy for P-body quantification; translational reporter assays","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic invalidation with rescue and phenotypic readout in somatic cells; preprint, not yet peer-reviewed","pmids":["bio_10.1101_2025.10.30.685488"],"is_preprint":true}],"current_model":"LSM14B is an RNA-binding protein with an N-terminal Lsm domain that forms RNP complexes in P-bodies, MARDOs, and stress granules; in oocytes it acts as an interaction hub that (1) represses translation of dormant mRNAs (e.g., cyclin B1) in a complex with DDX6 and CPEB1 via the 3'UTR to maintain prophase arrest, (2) activates translation of target mRNAs by interacting with the N-terminal RRM of Musashi1, (3) controls maternal mRNA storage and stability required for meiotic maturation and early embryogenesis, and (4) regulates P-body component expression/localization (including DDX6, LSM14A, DCP1A, 4E-T); in somatic cells LSM14B acts as a negative regulator of P-body assembly."},"narrative":{"mechanistic_narrative":"LSM14B is an oocyte-specific RNA-binding protein with an N-terminal Lsm domain that functions as a ribonucleoprotein interaction hub controlling the storage, stability, and translation of maternal mRNAs throughout oocyte development and early embryogenesis [PMID:37083226, PMID:37578641]. It partitions into membraneless compartments — P-body-like granules, stress-granule-like assemblies, and mitochondria-associated ribonucleoprotein domains (MARDO) — and its loss disrupts these granules, impairing maternal mRNA accumulation in non-growing oocytes and translational control in fully grown oocytes [PMID:22614839, PMID:37578641]. LSM14B exerts bidirectional translational control: within a DDX6–LSM14B–CPEB1 complex it represses cyclin B1 translation through the cyclin B1 3'UTR to maintain prophase arrest [PMID:39567493], while through its N-terminal RNA recognition motifs it binds Musashi1 to activate translation of target mRNAs [PMID:40211036]. Through these activities LSM14B governs the expression and localization of core P-body components including DDX6, LSM14A, DCP1A, and 4E-T [PMID:37481122], and is required for oocyte meiotic maturation, with its loss causing meiotic arrest, spindle and chromosome defects, and female-specific infertility [PMID:28458300, PMID:37083226, PMID:37578641]. In somatic epithelial cells LSM14B acts as a negative regulator of P-body assembly [PMID:bio_10.1101_2025.10.30.685488].","teleology":[{"year":2004,"claim":"Established LSM14B's existence as a distinct Lsm-domain protein, raising the possibility of a nucleic-acid-binding and cell-cycle-regulatory role before any experiment was done.","evidence":"Integrative bioinformatics and computational domain analysis","pmids":["15225602"],"confidence":"Low","gaps":["Computational prediction only with no experimental validation of binding or function","No localization or partner data","G2/M role inferred from yeast partners, not tested"]},{"year":2010,"claim":"Placed LSM14B inside a defined oocyte mRNP, answering whether it associates with the translational repression machinery by showing it co-purifies with CPEB and Xp54/DDX6.","evidence":"Co-immunoprecipitation of epitope-tagged Pat1 from Xenopus oocyte extracts identifying CPEB, Xp54, eIF4E1b, ePAB partners","pmids":["20826699"],"confidence":"Medium","gaps":["Association does not establish direct binding versus indirect complex membership","Functional consequence of the interactions not tested","Single organism (Xenopus)"]},{"year":2012,"claim":"Defined LSM14B's subcellular behavior, showing it localizes to P-bodies and can nucleate large mixed P-body/stress-granule assemblies.","evidence":"Fluorescence microscopy and marker immunostaining of expressed RAP55B in human cultured cells","pmids":["22614839"],"confidence":"Medium","gaps":["Based on overexpression, which may force granule formation","Endogenous localization not assessed","No mechanism for granule nucleation"]},{"year":2015,"claim":"Distinguished LSM14B functionally from its paralog by showing it associates with polysomes and translatable mRNAs, pointing toward a translational activation rather than repression role.","evidence":"Co-IP, polysome fractionation, and RNA binding assays in Xenopus oocytes","pmids":["26455898"],"confidence":"Medium","gaps":["Direct activation of specific mRNAs not demonstrated","Apparent contradiction with later repression role not resolved here","Single lab, Xenopus only"]},{"year":2017,"claim":"Provided the first loss-of-function evidence that LSM14B is required for meiotic maturation, linking it to cell-cycle progression via candidate targets Cyclin B1 and Cdc20.","evidence":"LSM14B knockdown in mouse oocytes with spindle/chromosome immunofluorescence and mRNA level analysis","pmids":["28458300"],"confidence":"Medium","gaps":["Targets identified by correlation, not direct binding or reporter assay","Mechanism of mRNA regulation unresolved","Knockdown rather than genetic null"]},{"year":2023,"claim":"Established LSM14B as an oocyte-specific RNA-binding interaction hub whose genetic loss causes female infertility, defining its physiological requirement across oogenesis and early embryogenesis.","evidence":"mRNA-interactome capture, Lsm14b knockout mouse, translation reporters, and proteomic interaction mapping","pmids":["37083226"],"confidence":"High","gaps":["Full identity of the bound mRNA and protein interactome not exhaustively resolved","Direct versus indirect translational effects not separated for all targets"]},{"year":2023,"claim":"Connected LSM14B to specific membraneless compartments (P-body-like granules and MARDO) and tied granule integrity to maternal mRNA stability and timely MPF activation.","evidence":"Conditional knockout mouse, scRNA-seq, bulk RNA-seq, immunostaining of granule components, and WEE1/2 inhibitor rescue","pmids":["37578641"],"confidence":"High","gaps":["Molecular basis for LSM14B-dependent granule assembly not defined","How granule dissolution links mechanistically to translation onset unresolved"]},{"year":2023,"claim":"Showed LSM14B controls the expression and localization of core P-body machinery, including DDX6, LSM14A, DCP1A, and 4E-T, placing it upstream of P-body composition in oocytes.","evidence":"Lsm14b knockout mouse, global transcriptome analysis, and immunostaining/localization analysis of P-body components","pmids":["37481122"],"confidence":"High","gaps":["Whether effects on DDX6 nuclear accumulation are direct or secondary unclear","Mechanism restraining aberrant transcriptional activation not defined"]},{"year":2024,"claim":"Resolved a direct mechanism of translational repression, showing a DDX6–LSM14B–CPEB1 complex silences cyclin B1 via its 3'UTR to hold oocytes in prophase arrest.","evidence":"Trim-Away depletion of each component, cyclin B1 translational reporter, and 3'UTR RNA interaction assay in mouse oocytes","pmids":["39567493"],"confidence":"High","gaps":["Stoichiometry and assembly order of the tripartite complex not defined","Whether LSM14B binds the 3'UTR directly or through CPEB1 not separated"]},{"year":2024,"claim":"Demonstrated LSM14B is a physiological mediator of oocyte quality by showing its restoration rescues translation, mitochondrial, and meiotic defects in metabolically stressed oocytes.","evidence":"siRNA knockdown and Lsm14b mRNA rescue injection in mouse oocytes with RNA-seq and mitochondrial/meiotic assays","pmids":["38552928"],"confidence":"Medium","gaps":["Direct LSM14B targets driving mitochondrial phenotype not identified","Link between mRNA storage defects and mitochondrial dysfunction mechanistically incomplete"]},{"year":2025,"claim":"Defined the molecular basis of LSM14B-mediated translational activation, mapping a Musashi1 interaction to its N-terminal RRMs and showing it is required for Musashi1-dependent activation of target mRNAs.","evidence":"Co-IP, domain-mapping mutagenesis, translational reporters in Xenopus oocytes, and validation on mammalian Prop1 mRNA","pmids":["40211036"],"confidence":"High","gaps":["How LSM14B switches between repressive and activating complexes not resolved","Full set of Musashi1/LSM14B co-activated mRNAs unknown"]},{"year":2025,"claim":"Extended LSM14B function to somatic cells, showing it negatively regulates P-body formation and that its glucocorticoid-driven loss promotes P-body accumulation and AU-rich mRNA sequestration.","evidence":"Genetic invalidation and rescue, FDA-approved drug screen, P-body quantification microscopy, and translational reporters (preprint)","pmids":["bio_10.1101_2025.10.30.685488"],"confidence":"Medium","gaps":["Preprint, not yet peer-reviewed","Mechanism by which LSM14B restrains P-body assembly in somatic cells undefined","Direct AU-rich mRNA targets not enumerated"]},{"year":null,"claim":"How LSM14B is partitioned between repressive (DDX6/CPEB1) and activating (Musashi1) complexes, and what determines its switch between promoting and restraining granule assembly across oocyte and somatic contexts, remains unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No structural model of LSM14B complexes","Regulatory signals controlling complex choice unknown","Direct RNA-binding specificity of the Lsm domain not mapped"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[6,9,11]},{"term_id":"GO:0045182","term_label":"translation regulator activity","supporting_discovery_ids":[9,11]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[6,9,11]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[3,7]},{"term_id":"GO:0005739","term_label":"mitochondrion","supporting_discovery_ids":[7]}],"pathway":[{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[6,7,9]},{"term_id":"R-HSA-1474165","term_label":"Reproduction","supporting_discovery_ids":[6,7]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[5,9]}],"complexes":["DDX6-LSM14B-CPEB1 cyclin B1 repression complex","CPEB RNP complex","P-body","MARDO (mitochondria-associated ribonucleoprotein domain)"],"partners":["DDX6","CPEB1","MSI1","LSM14A","DCP1A","EIF4ENIF1","EIF4E1B"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9BX40","full_name":"Protein LSM14 homolog B","aliases":["RNA-associated protein 55B","hRAP55B"],"length_aa":385,"mass_kda":42.1,"function":"mRNA-binding protein essential for female fertility, oocyte meiotic maturation and the assembly of MARDO (mitochondria-associated ribonucleoprotein domain), a membraneless compartment that stores maternal mRNAs in oocytes. Ensures the proper accumulation and clearance of mRNAs essential for oocyte meiotic maturation and the normal progression from Meiosis I to Meiosis II in oocytes. Promotes the translation of some oogenesis-related mRNAs. Regulates the expression and/or localization of some key P-body proteins in oocytes. Essential for the assembly of the primordial follicle in the ovary","subcellular_location":"Cytoplasm, Cytoplasmic ribonucleoprotein granule","url":"https://www.uniprot.org/uniprotkb/Q9BX40/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/LSM14B","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000149657","cell_line_id":"CID001689","localizations":[{"compartment":"big_aggregates","grade":3},{"compartment":"cytoplasmic","grade":1}],"interactors":[{"gene":"DDX6","stoichiometry":4.0},{"gene":"LGALS1","stoichiometry":4.0},{"gene":"LSM14A","stoichiometry":4.0},{"gene":"YBX1","stoichiometry":0.2},{"gene":"C1QBP","stoichiometry":0.2},{"gene":"LBR","stoichiometry":0.2},{"gene":"EIF4ENIF1","stoichiometry":0.2},{"gene":"POLDIP2","stoichiometry":0.2},{"gene":"CLPX","stoichiometry":0.2},{"gene":"CSDE1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID001689","total_profiled":1310},"omim":[{"mim_id":"620689","title":"LSM FAMILY, MEMBER 14B; LSM14B","url":"https://www.omim.org/entry/620689"},{"mim_id":"611520","title":"POLYMERASE DELTA-INTERACTING PROTEIN 3; POLDIP3","url":"https://www.omim.org/entry/611520"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Vesicles","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/LSM14B"},"hgnc":{"alias_symbol":["FT005","bA11M20.3","FLJ25473","LSM13","RAP55B"],"prev_symbol":["C20orf40","FAM61B"]},"alphafold":{"accession":"Q9BX40","domains":[{"cath_id":"2.30.30.100","chopping":"11-78","consensus_level":"high","plddt":96.4338,"start":11,"end":78}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9BX40","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9BX40-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9BX40-F1-predicted_aligned_error_v6.png","plddt_mean":62.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=LSM14B","jax_strain_url":"https://www.jax.org/strain/search?query=LSM14B"},"sequence":{"accession":"Q9BX40","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9BX40.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9BX40/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9BX40"}},"corpus_meta":[{"pmid":"15225602","id":"PMC_15225602","title":"Novel Sm-like proteins with long C-terminal tails and associated methyltransferases.","date":"2004","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/15225602","citation_count":75,"is_preprint":false},{"pmid":"20826699","id":"PMC_20826699","title":"Distinct functions of maternal and somatic Pat1 protein paralogs.","date":"2010","source":"RNA (New York, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/20826699","citation_count":53,"is_preprint":false},{"pmid":"22614839","id":"PMC_22614839","title":"PRMT1 is required for RAP55 to localize to processing bodies.","date":"2012","source":"RNA biology","url":"https://pubmed.ncbi.nlm.nih.gov/22614839","citation_count":44,"is_preprint":false},{"pmid":"18723115","id":"PMC_18723115","title":"RAP55: insights into an evolutionarily conserved protein family.","date":"2008","source":"The international journal of biochemistry & cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/18723115","citation_count":42,"is_preprint":false},{"pmid":"37083226","id":"PMC_37083226","title":"LSM14B is an Oocyte-Specific RNA-Binding Protein Indispensable for Maternal mRNA Metabolism and Oocyte Development in Mice.","date":"2023","source":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/37083226","citation_count":32,"is_preprint":false},{"pmid":"33318146","id":"PMC_33318146","title":"Loss of ESRP1 blocks mouse oocyte development and leads to female infertility.","date":"2021","source":"Development (Cambridge, England)","url":"https://pubmed.ncbi.nlm.nih.gov/33318146","citation_count":32,"is_preprint":false},{"pmid":"35646684","id":"PMC_35646684","title":"Identification of LSM Family Members as Novel Unfavorable Biomarkers in Hepatocellular Carcinoma.","date":"2022","source":"Frontiers in 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Molecular basis of disease","url":"https://pubmed.ncbi.nlm.nih.gov/40139411","citation_count":6,"is_preprint":false},{"pmid":"40211036","id":"PMC_40211036","title":"Musashi-dependent mRNA translational activation is mediated through association with the Scd6/Like-sm family member, LSM14B.","date":"2025","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/40211036","citation_count":5,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.10.30.685488","title":"Glucocorticoids Modulate mRNA Translation Fate Through P-Body Dynamics","date":"2025-10-31","source":"bioRxiv","url":"https://doi.org/10.1101/2025.10.30.685488","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10522,"output_tokens":3359,"usd":0.040975,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10908,"output_tokens":4000,"usd":0.07727,"stage2_stop_reason":"end_turn"},"total_usd":0.118245,"stage1_batch_id":"msgbatch_01BbTCMyrRPyhtEq6b1MdwCN","stage2_batch_id":"msgbatch_011dEed5bbxYvTAaQWKJevxu","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2004,\n      \"finding\": \"LSM14B (Lsm13/RAP55B) was identified as a novel Lsm domain protein with a long C-terminal tail, containing an N-terminal Lsm domain predicted to bind nucleic acids; computational analysis suggested involvement in regulation of the mitotic G2/M phase based on known yeast interaction partners.\",\n      \"method\": \"Integrative bioinformatics / computational domain analysis\",\n      \"journal\": \"FEBS letters\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational prediction only, no experimental validation of binding or function\",\n      \"pmids\": [\"15225602\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"RAP55B (LSM14B) shares multiple conserved domains with RAP55A including the LSm14 domain, serine/threonine-rich region, FDF motif, FFD-TFG box, and RGG repeats; Xenopus RAP55B (xRAP55B) was shown to be part of translationally repressed mRNP complexes in early oocytes.\",\n      \"method\": \"Sequence analysis and biochemical characterization of mRNP complexes in Xenopus oocytes\",\n      \"journal\": \"The international journal of biochemistry & cell biology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — domain characterization and mRNP association reported in a review/analysis paper with limited experimental detail in abstract\",\n      \"pmids\": [\"18723115\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"RAP55B (LSM14B) was identified as a component of the CPEB RNP complex in Xenopus oocytes, interacting with CPEB, Xp54, eIF4E1b, and ePAB; epitope-tagged xPat1 proteins co-immunoprecipitated RAP55B from oocyte extracts.\",\n      \"method\": \"Co-immunoprecipitation of epitope-tagged Pat1 proteins from Xenopus oocyte extracts\",\n      \"journal\": \"RNA (New York, N.Y.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — Co-IP from oocyte extracts with multiple interaction partners identified; single lab but confirmed in a broader complex context\",\n      \"pmids\": [\"20826699\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"RAP55B (LSM14B) localizes to processing bodies (P-bodies) when expressed in human cultured cells; high-level expression of RAP55B induces formation of SG-like large cytoplasmic mRNP granules that contain both P-body and stress granule components.\",\n      \"method\": \"Fluorescence microscopy of expressed RAP55B in human cultured cells; immunostaining for P-body and SG markers\",\n      \"journal\": \"RNA biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization experiment with functional consequence (granule assembly), single lab, two orthogonal readouts\",\n      \"pmids\": [\"22614839\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"Xenopus RAPB (xRAPB, LSM14B ortholog) specifically interacts with the DDX6 helicase Xp54; unlike xRAPA, xRAPB is detected in polysomes and stalled translation initiation complexes and its overexpression leads to selective binding to translatable mRNA species without causing translation repression or mRNA degradation, suggesting a role in mRNA translational activation rather than repression.\",\n      \"method\": \"Co-immunoprecipitation, polysome fractionation, RNA binding assays in Xenopus oocytes\",\n      \"journal\": \"Biochimica et biophysica acta\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal biochemical evidence (Co-IP, polysome profiling) in a single lab with multiple orthogonal methods\",\n      \"pmids\": [\"26455898\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"LSM14B is essential for oocyte meiotic maturation in mice; knockdown/loss of LSM14B causes meiotic arrest at metaphase, chromosome misalignment, and abnormal spindle assembly checkpoint (SAC) and maturation promoting factor (MPF) activation; Cyclin B1 and Cdc20 mRNAs were identified as likely direct targets whose levels changed with LSM14B expression.\",\n      \"method\": \"LSM14B knockdown in mouse oocytes; immunofluorescence for spindle and chromosome organization; mRNA level analysis\",\n      \"journal\": \"The Journal of reproduction and development\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function with defined cellular phenotype and identification of mRNA targets; single lab\",\n      \"pmids\": [\"28458300\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"LSM14B is an oocyte-specific RNA-binding protein that acts as an interaction hub for proteins and mRNAs throughout oocyte development; deletion of Lsm14b causes female-specific infertility with oocytes unable to complete meiosis or support early embryogenesis; LSM14B regulates translation of a subset of its bound mRNAs; RNP complexes tethered by LSM14B are exclusive to oocytes.\",\n      \"method\": \"mRNA-interactome capture to identify oocyte RBPs; Lsm14b knockout mouse model; translation reporter assays; proteomic interaction studies\",\n      \"journal\": \"Advanced science (Weinheim, Baden-Wurttemberg, Germany)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic knockout with defined infertility phenotype, mRNA-interactome capture, proteomic interaction mapping; multiple orthogonal methods in a single comprehensive study\",\n      \"pmids\": [\"37083226\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"LSM14B is a component of membraneless compartments including P-body-like granules and mitochondria-associated ribonucleoprotein domains (MARDO) in germ cells; loss of LSM14B disrupts primordial follicle assembly, impairs maternal mRNA accumulation and stability in non-growing oocytes (concomitant with impaired P-body-like granule assembly), and disrupts translation in fully grown oocytes associated with dissolution of MARDO components; Lsm14b-deficient oocytes show compromised maturation promoting factor activation that can be rescued by WEE1/2 inhibitor.\",\n      \"method\": \"Lsm14b conditional knockout mouse; 10x Genomics single-cell RNA-seq; RNA-seq of GV-stage oocytes; immunostaining for P-body and MARDO components; WEE1/2 inhibitor rescue experiment\",\n      \"journal\": \"Cellular and molecular life sciences : CMLS\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic knockout with multiple orthogonal methods (scRNA-seq, bulk RNA-seq, immunostaining, pharmacological rescue), single lab but comprehensive\",\n      \"pmids\": [\"37578641\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"LSM14B regulates oocyte maturation through control of P-body function; loss of LSM14B in mouse ovaries causes aberrant transcriptional activation (altered non-surrounded nucleolus/surrounded nucleolus oocyte proportions), abnormal chromosome assembly and segregation, and changes in expression/localization of P-body components LSM14A, DCP1A, and 4E-T; DDX6 is downregulated and abnormally accumulates in the nucleus in Lsm14b-deficient oocytes.\",\n      \"method\": \"Lsm14b knockout mouse; global transcriptome analysis; immunostaining for P-body components; nuclear/cytoplasmic localization analysis of DDX6\",\n      \"journal\": \"Journal of genetics and genomics = Yi chuan xue bao\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic knockout with transcriptome analysis and immunostaining for specific pathway components; multiple orthogonal methods\",\n      \"pmids\": [\"37481122\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"A complex of DDX6, LSM14B, and CPEB1 directly represses cyclin B1 translation in mouse oocytes through interaction with the cyclin B1 3'UTR, thereby maintaining prophase arrest; this was demonstrated using Trim-Away protein depletion of each component.\",\n      \"method\": \"Trim-Away depletion of DDX6, LSM14B, and CPEB1 in mouse oocytes; translational reporter assay for cyclin B1; RNA interaction assay with 3'UTR\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — Trim-Away protein depletion with translational reporter and defined 3'UTR interaction; multiple proteins tested with phenotypic rescue; published in high-quality journal\",\n      \"pmids\": [\"39567493\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"LSM14B knockdown in oocytes from normal-diet mice recapitulates translation defects, mitochondrial dysfunction, and meiotic defects seen in obese mice; injection of Lsm14b mRNA into oocytes from high-fat diet mice rescues these phenotypes, establishing that LSM14B mediates maternal mRNA storage and translation required for oocyte quality.\",\n      \"method\": \"siRNA knockdown and mRNA rescue injection in mouse oocytes; RNA-seq; functional assays for mitochondrial function and meiotic progression\",\n      \"journal\": \"Free radical biology & medicine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function and gain-of-function rescue experiment with defined phenotypic readouts; single lab\",\n      \"pmids\": [\"38552928\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"LSM14B physically associates with Musashi1 through its N-terminal RNA recognition motifs (not the C-terminal domain used by other Musashi partners) and is required for Musashi1-dependent translational activation of target mRNAs during Xenopus oocyte maturation; LSM14B also mediates Musashi1-dependent translational activation of the mammalian Prop1 mRNA.\",\n      \"method\": \"Co-immunoprecipitation; domain mapping by mutagenesis; translational reporter assays in Xenopus oocytes; rescue experiments\",\n      \"journal\": \"Scientific reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP with domain mapping, functional rescue assay, and mammalian mRNA target validation; multiple orthogonal methods in one study\",\n      \"pmids\": [\"40211036\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"LSM14B acts as a negative regulator of P-body formation in somatic epithelial cells; glucocorticoid treatment decreases LSM14B levels and this decrease is linked to P-body accumulation and sequestration of AU-rich mRNAs, reducing their translation yield.\",\n      \"method\": \"Genetic invalidation and rescue of LSM14B; FDA-approved drug screen; fluorescence microscopy for P-body quantification; translational reporter assays\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic invalidation with rescue and phenotypic readout in somatic cells; preprint, not yet peer-reviewed\",\n      \"pmids\": [\"bio_10.1101_2025.10.30.685488\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"LSM14B is an RNA-binding protein with an N-terminal Lsm domain that forms RNP complexes in P-bodies, MARDOs, and stress granules; in oocytes it acts as an interaction hub that (1) represses translation of dormant mRNAs (e.g., cyclin B1) in a complex with DDX6 and CPEB1 via the 3'UTR to maintain prophase arrest, (2) activates translation of target mRNAs by interacting with the N-terminal RRM of Musashi1, (3) controls maternal mRNA storage and stability required for meiotic maturation and early embryogenesis, and (4) regulates P-body component expression/localization (including DDX6, LSM14A, DCP1A, 4E-T); in somatic cells LSM14B acts as a negative regulator of P-body assembly.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"LSM14B is an oocyte-specific RNA-binding protein with an N-terminal Lsm domain that functions as a ribonucleoprotein interaction hub controlling the storage, stability, and translation of maternal mRNAs throughout oocyte development and early embryogenesis [#6, #7]. It partitions into membraneless compartments — P-body-like granules, stress-granule-like assemblies, and mitochondria-associated ribonucleoprotein domains (MARDO) — and its loss disrupts these granules, impairing maternal mRNA accumulation in non-growing oocytes and translational control in fully grown oocytes [#3, #7]. LSM14B exerts bidirectional translational control: within a DDX6–LSM14B–CPEB1 complex it represses cyclin B1 translation through the cyclin B1 3'UTR to maintain prophase arrest [#9], while through its N-terminal RNA recognition motifs it binds Musashi1 to activate translation of target mRNAs [#11]. Through these activities LSM14B governs the expression and localization of core P-body components including DDX6, LSM14A, DCP1A, and 4E-T [#8], and is required for oocyte meiotic maturation, with its loss causing meiotic arrest, spindle and chromosome defects, and female-specific infertility [#5, #6, #7]. In somatic epithelial cells LSM14B acts as a negative regulator of P-body assembly [#12].\",\n  \"teleology\": [\n    {\n      \"year\": 2004,\n      \"claim\": \"Established LSM14B's existence as a distinct Lsm-domain protein, raising the possibility of a nucleic-acid-binding and cell-cycle-regulatory role before any experiment was done.\",\n      \"evidence\": \"Integrative bioinformatics and computational domain analysis\",\n      \"pmids\": [\"15225602\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Computational prediction only with no experimental validation of binding or function\", \"No localization or partner data\", \"G2/M role inferred from yeast partners, not tested\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Placed LSM14B inside a defined oocyte mRNP, answering whether it associates with the translational repression machinery by showing it co-purifies with CPEB and Xp54/DDX6.\",\n      \"evidence\": \"Co-immunoprecipitation of epitope-tagged Pat1 from Xenopus oocyte extracts identifying CPEB, Xp54, eIF4E1b, ePAB partners\",\n      \"pmids\": [\"20826699\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Association does not establish direct binding versus indirect complex membership\", \"Functional consequence of the interactions not tested\", \"Single organism (Xenopus)\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Defined LSM14B's subcellular behavior, showing it localizes to P-bodies and can nucleate large mixed P-body/stress-granule assemblies.\",\n      \"evidence\": \"Fluorescence microscopy and marker immunostaining of expressed RAP55B in human cultured cells\",\n      \"pmids\": [\"22614839\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Based on overexpression, which may force granule formation\", \"Endogenous localization not assessed\", \"No mechanism for granule nucleation\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Distinguished LSM14B functionally from its paralog by showing it associates with polysomes and translatable mRNAs, pointing toward a translational activation rather than repression role.\",\n      \"evidence\": \"Co-IP, polysome fractionation, and RNA binding assays in Xenopus oocytes\",\n      \"pmids\": [\"26455898\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct activation of specific mRNAs not demonstrated\", \"Apparent contradiction with later repression role not resolved here\", \"Single lab, Xenopus only\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Provided the first loss-of-function evidence that LSM14B is required for meiotic maturation, linking it to cell-cycle progression via candidate targets Cyclin B1 and Cdc20.\",\n      \"evidence\": \"LSM14B knockdown in mouse oocytes with spindle/chromosome immunofluorescence and mRNA level analysis\",\n      \"pmids\": [\"28458300\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Targets identified by correlation, not direct binding or reporter assay\", \"Mechanism of mRNA regulation unresolved\", \"Knockdown rather than genetic null\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Established LSM14B as an oocyte-specific RNA-binding interaction hub whose genetic loss causes female infertility, defining its physiological requirement across oogenesis and early embryogenesis.\",\n      \"evidence\": \"mRNA-interactome capture, Lsm14b knockout mouse, translation reporters, and proteomic interaction mapping\",\n      \"pmids\": [\"37083226\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Full identity of the bound mRNA and protein interactome not exhaustively resolved\", \"Direct versus indirect translational effects not separated for all targets\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Connected LSM14B to specific membraneless compartments (P-body-like granules and MARDO) and tied granule integrity to maternal mRNA stability and timely MPF activation.\",\n      \"evidence\": \"Conditional knockout mouse, scRNA-seq, bulk RNA-seq, immunostaining of granule components, and WEE1/2 inhibitor rescue\",\n      \"pmids\": [\"37578641\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis for LSM14B-dependent granule assembly not defined\", \"How granule dissolution links mechanistically to translation onset unresolved\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Showed LSM14B controls the expression and localization of core P-body machinery, including DDX6, LSM14A, DCP1A, and 4E-T, placing it upstream of P-body composition in oocytes.\",\n      \"evidence\": \"Lsm14b knockout mouse, global transcriptome analysis, and immunostaining/localization analysis of P-body components\",\n      \"pmids\": [\"37481122\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether effects on DDX6 nuclear accumulation are direct or secondary unclear\", \"Mechanism restraining aberrant transcriptional activation not defined\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Resolved a direct mechanism of translational repression, showing a DDX6–LSM14B–CPEB1 complex silences cyclin B1 via its 3'UTR to hold oocytes in prophase arrest.\",\n      \"evidence\": \"Trim-Away depletion of each component, cyclin B1 translational reporter, and 3'UTR RNA interaction assay in mouse oocytes\",\n      \"pmids\": [\"39567493\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Stoichiometry and assembly order of the tripartite complex not defined\", \"Whether LSM14B binds the 3'UTR directly or through CPEB1 not separated\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Demonstrated LSM14B is a physiological mediator of oocyte quality by showing its restoration rescues translation, mitochondrial, and meiotic defects in metabolically stressed oocytes.\",\n      \"evidence\": \"siRNA knockdown and Lsm14b mRNA rescue injection in mouse oocytes with RNA-seq and mitochondrial/meiotic assays\",\n      \"pmids\": [\"38552928\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct LSM14B targets driving mitochondrial phenotype not identified\", \"Link between mRNA storage defects and mitochondrial dysfunction mechanistically incomplete\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Defined the molecular basis of LSM14B-mediated translational activation, mapping a Musashi1 interaction to its N-terminal RRMs and showing it is required for Musashi1-dependent activation of target mRNAs.\",\n      \"evidence\": \"Co-IP, domain-mapping mutagenesis, translational reporters in Xenopus oocytes, and validation on mammalian Prop1 mRNA\",\n      \"pmids\": [\"40211036\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How LSM14B switches between repressive and activating complexes not resolved\", \"Full set of Musashi1/LSM14B co-activated mRNAs unknown\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Extended LSM14B function to somatic cells, showing it negatively regulates P-body formation and that its glucocorticoid-driven loss promotes P-body accumulation and AU-rich mRNA sequestration.\",\n      \"evidence\": \"Genetic invalidation and rescue, FDA-approved drug screen, P-body quantification microscopy, and translational reporters (preprint)\",\n      \"pmids\": [\"bio_10.1101_2025.10.30.685488\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Preprint, not yet peer-reviewed\", \"Mechanism by which LSM14B restrains P-body assembly in somatic cells undefined\", \"Direct AU-rich mRNA targets not enumerated\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How LSM14B is partitioned between repressive (DDX6/CPEB1) and activating (Musashi1) complexes, and what determines its switch between promoting and restraining granule assembly across oocyte and somatic contexts, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No structural model of LSM14B complexes\", \"Regulatory signals controlling complex choice unknown\", \"Direct RNA-binding specificity of the Lsm domain not mapped\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [6, 9, 11]},\n      {\"term_id\": \"GO:0045182\", \"supporting_discovery_ids\": [9, 11]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [6, 9, 11]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [3, 7]},\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [7]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [6, 7, 9]},\n      {\"term_id\": \"R-HSA-1474165\", \"supporting_discovery_ids\": [6, 7]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [5, 9]}\n    ],\n    \"complexes\": [\n      \"DDX6-LSM14B-CPEB1 cyclin B1 repression complex\",\n      \"CPEB RNP complex\",\n      \"P-body\",\n      \"MARDO (mitochondria-associated ribonucleoprotein domain)\"\n    ],\n    \"partners\": [\n      \"DDX6\",\n      \"CPEB1\",\n      \"MSI1\",\n      \"LSM14A\",\n      \"DCP1A\",\n      \"EIF4ENIF1\",\n      \"EIF4E1B\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}