{"gene":"STRIP1","run_date":"2026-04-28T21:42:57","timeline":{"discoveries":[{"year":2008,"finding":"STRIP1 (formerly FAM40A) is a novel component of the STRIPAK complex, a large multiprotein assembly containing PP2A catalytic and scaffolding subunits, striatins (PP2A regulatory B''' subunits), Mob3, STRIP2, CCM3, and germinal center kinase III family kinases; STRIPAK establishes mutually exclusive interactions with either CTTNBP2 proteins or a subcomplex of SLMAP/SIKE/FGFR1OP2.","method":"Iterative affinity purification/mass spectrometry (AP-MS) interaction network mapping","journal":"Molecular & cellular proteomics : MCP","confidence":"High","confidence_rationale":"Tier 2 — large-scale AP-MS with reciprocal validation, foundational discovery replicated widely","pmids":["18782753"],"is_preprint":false},{"year":2011,"finding":"FAM40A (STRIP1) depletion reduces cell spreading, whereas FAM40B (STRIP2) depletion induces cell elongation and tail retraction defects, identifying STRIP1 as a regulator of cell morphology and cytoskeletal organization distinct from its paralog.","method":"Genome-wide RNAi screen in Drosophila cells followed by siRNA knockdown in human cells with morphological phenotyping and actin filament imaging","journal":"BMC biology","confidence":"Medium","confidence_rationale":"Tier 2 — clean KD with defined cellular phenotype, but single lab","pmids":["21834987"],"is_preprint":false},{"year":2012,"finding":"Yeast Far11, the ortholog of mammalian STRIP1/FAM40A, genetically antagonizes TORC2 signaling; Far11 interacts with PP2A subunits Tpd3 and Pph21, and deletion of Far11 restores phosphorylation of the TORC2 substrate Slm1 in tor2-21 mutants, placing the PP2A-Far11 complex as a negative regulator of TORC2.","method":"Genetic suppressor screen, co-immunoprecipitation, phosphorylation assays in Saccharomyces cerevisiae","journal":"Genetics","confidence":"Medium","confidence_rationale":"Tier 2 — epistasis and biochemical interaction in yeast ortholog, single lab","pmids":["22298706"],"is_preprint":false},{"year":2014,"finding":"FAM40A (STRIP1) negatively regulates the MST3 and MST4 kinases within the STRIPAK complex; loss of FAM40A results in co-localization of contractile actomyosin machinery with ERM proteins via MST3/4-mediated phosphorylation of PPP1R14A-D (inhibitors of PPP1CB), thereby controlling the mode of cancer cell migration.","method":"siRNA knockdown, in vitro kinase assays, computational modeling, in vitro migration assays, in vivo breast cancer metastasis assays; FAM40B tumor-derived mutations shown to uncouple it from PP2A","journal":"Nature cell biology","confidence":"High","confidence_rationale":"Tier 1-2 — multiple orthogonal methods including in vivo metastasis, kinase assays, and mutagenesis; high citation count","pmids":["25531779"],"is_preprint":false},{"year":2017,"finding":"Strip1 is essential for mesoderm cell migration in vivo; Strip1-null mouse embryos show defects in mesoderm organization and axial extension correlated with decreased cell spreading, abnormal focal adhesions, disorganized actin cytoskeleton, and decreased migration velocity in cultured mesoderm explants and MEFs.","method":"Mouse knockout, cultured mesoderm explants, mouse embryonic fibroblasts, live imaging, immunofluorescence for focal adhesions and actin","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 2 — clean KO with defined in vivo and ex vivo cellular phenotypes, multiple orthogonal readouts","pmids":["29203676"],"is_preprint":false},{"year":2018,"finding":"FAM40A and FAM40B interact with CCM3 and regulate endothelial cell contractility; knockdown of FAM40A or FAM40B increases stress fibers and reduces angiogenic loop formation, phenotypes that are rescued by ROCK inhibition, placing FAM40A/B upstream of Rho-ROCK signaling in endothelial cells.","method":"Co-immunoprecipitation, RNAi knockdown, in vitro angiogenesis assay, pharmacological ROCK inhibition rescue","journal":"BMC cell biology","confidence":"Medium","confidence_rationale":"Tier 2-3 — Co-IP plus functional rescue, single lab","pmids":["30509168"],"is_preprint":false},{"year":2019,"finding":"STRIP1 forms one of two 'arms' in the STRIPAK complex that loads MST2 onto the complex in a phosphorylation-dependent manner; decreased cell density triggers dissociation of the STRIP1 arm from STRIPAK, reflecting dynamic assembly upon upstream signal sensing, while disrupting this interface abrogates STRIPAK's regulatory effect on Hippo signaling.","method":"Crystallography, biochemical reconstitution, co-immunoprecipitation, cell density-dependent dissociation assays, mutagenesis of interface residues","journal":"Cell discovery","confidence":"High","confidence_rationale":"Tier 1 — crystallographic structure plus biochemical reconstitution and functional mutagenesis","pmids":["30622739"],"is_preprint":false},{"year":2020,"finding":"Loss of STRIP1 in breast cancer cells causes cell cycle arrest via induction of CDK inhibitors p21 and p27; the p21/γH2AX ratio imbalance caused by STRIP1 loss can be rescued by co-depletion of MST3 and MST4 kinases, placing STRIP1 upstream of MST3/4 in controlling p21-mediated cell cycle exit.","method":"siRNA knockdown, flow cytometry, single-cell immunofluorescence for p21 and γH2AX, epistasis by double knockdown","journal":"Frontiers in cell and developmental biology","confidence":"Medium","confidence_rationale":"Tier 2 — epistasis by double KD with quantitative single-cell readouts, single lab","pmids":["32258031"],"is_preprint":false},{"year":2021,"finding":"Cryo-EM structure of the human STRIPAK core (PP2AA, PP2AC, STRN3, STRIP1, MOB4) at 3.2-Å resolution reveals a noncanonical PP2A assembly with four copies of STRN3 forming an elongated homotetrameric scaffold; an inositol hexakisphosphate (IP6) is a structural cofactor of STRIP1; mutations at subunit interfaces disrupt complex integrity and cause aberrant Hippo pathway activation.","method":"Cryo-EM structure determination, mutagenesis of interface residues, Hippo pathway reporter assays","journal":"Nature structural & molecular biology","confidence":"High","confidence_rationale":"Tier 1 — high-resolution cryo-EM structure with mutagenesis and functional validation","pmids":["33633399"],"is_preprint":false},{"year":2022,"finding":"Zebrafish Strip1 physically interacts with Striatin 3 (Strn3) within STRIPAK and is required for retinal ganglion cell (RGC) survival; loss of Strip1 or Strn3 activates the pro-apoptotic transcription factor Jun in RGCs, and Jun knockdown rescues RGC survival in strip1 mutants, placing Strip1 upstream of Jun-mediated apoptosis in inner retinal circuit formation.","method":"Zebrafish loss-of-function genetics, co-immunoprecipitation, immunofluorescence, epistasis by morpholino-mediated Jun knockdown","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 — in vivo genetic epistasis with biochemical interaction, multiple orthogonal methods","pmids":["35314028"],"is_preprint":false},{"year":2023,"finding":"C. elegans FARL-11 (STRIP1/2 ortholog) and CASH-1 (striatin) form a complex in vivo, both localize to the sarcoplasmic reticulum (SR) in muscle, and missense mutations in farl-11 or cash-1 disrupt SR organization around M-lines and alter levels of the SR Ca2+ release channel UNC-68, demonstrating a role for the STRIPAK complex in SR/ER organization.","method":"Co-immunoprecipitation, immunofluorescence localization, missense mutant characterization, immunoblot for UNC-68 levels in C. elegans","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 2 — direct localization with functional consequence, in vivo complex formation, ortholog system","pmids":["37314837"],"is_preprint":false},{"year":2016,"finding":"C. elegans FARL-11 (STRIP1/2 ortholog) localizes to the ER and is required for cell cycle-dependent ER morphological changes in embryos and for proper membrane localization of the GLP-1/Notch receptor in the germline, linking STRIPAK to ER dynamics and receptor trafficking.","method":"Fluorescence localization, RNAi/genetic loss-of-function, live imaging of ER morphology, GLP-1 receptor localization assay in C. elegans","journal":"Development (Cambridge, England)","confidence":"Medium","confidence_rationale":"Tier 2 — direct localization tied to functional consequence, ortholog system","pmids":["27510976"],"is_preprint":false},{"year":2026,"finding":"Strip1 localizes to the nucleolus in neonatal rat ventricular cardiomyocytes and associates with cardiac STRIPAK complex; Strip1 knockdown induces cardiomyocyte hypertrophy and activates MST1/MST2 and MST4 kinases as well as Calcineurin/NFAT pro-hypertrophic signaling; morpholino-driven Strip1 reduction in zebrafish causes impaired cardiac function.","method":"siRNA knockdown in NRVCMs, immunofluorescence localization, zebrafish morpholino knockdown, kinase activity assays, NFAT reporter assays","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 — multiple orthogonal methods, in vitro and in vivo, single lab","pmids":["41892331"],"is_preprint":false}],"current_model":"STRIP1 is a core structural component of the STRIPAK complex — a noncanonical PP2A holoenzyme in which STRIP1 forms one of two arms anchoring MST-family kinases to a homotetrameric STRN3 scaffold (with IP6 as a STRIP1 cofactor) — and acts as a negative regulator of MST3/4 kinase activity, thereby controlling actomyosin contractility, cell migration, ER/SR organization, and Hippo/Hippo-adjacent (Jun, Calcineurin/NFAT) pro-apoptotic and pro-hypertrophic signaling in a context-dependent, cell-density-responsive manner."},"narrative":{"teleology":[{"year":2008,"claim":"Identification of STRIP1 as a novel STRIPAK subunit resolved the composition of a previously uncharacterized PP2A-striatin supercomplex and revealed mutually exclusive sub-assemblies within it.","evidence":"Iterative AP-MS with reciprocal bait validations in mammalian cells","pmids":["18782753"],"confidence":"High","gaps":["Functional role of STRIP1 within the complex was unknown","Stoichiometry and architecture of the complex were unresolved","No disease or organismal phenotype yet linked"]},{"year":2011,"claim":"RNAi screening established that STRIP1 and its paralog STRIP2 have non-redundant roles in cell morphology, with STRIP1 specifically required for normal cell spreading.","evidence":"Genome-wide Drosophila RNAi screen followed by human siRNA knockdown with morphological and actin cytoskeletal phenotyping","pmids":["21834987"],"confidence":"Medium","gaps":["Molecular target through which STRIP1 controls spreading was not identified","Single-lab finding not independently confirmed at the time"]},{"year":2012,"claim":"Genetic epistasis in yeast placed the STRIP1 ortholog Far11 as a negative regulator of TORC2 signaling via PP2A, providing the first pathway-level positioning of STRIP1-family proteins.","evidence":"Suppressor screen, co-immunoprecipitation, and phosphorylation assays in S. cerevisiae","pmids":["22298706"],"confidence":"Medium","gaps":["Whether mammalian STRIP1 similarly antagonizes mTORC2 was untested","Mechanism of PP2A substrate selection was unclear"]},{"year":2014,"claim":"Mechanistic dissection revealed that STRIP1 restrains MST3/4 kinase activity within STRIPAK, and that its loss hyperactivates a MST3/4→PPP1R14A→actomyosin contractility axis that alters cancer cell migration mode and metastasis in vivo.","evidence":"siRNA, in vitro kinase assays, computational modeling, in vitro migration, and in vivo breast cancer metastasis assays with mutagenesis","pmids":["25531779"],"confidence":"High","gaps":["Structural basis of STRIP1-mediated kinase inhibition was unknown","Whether STRIP1 directly contacts MST3/4 or acts through PP2A catalytic activity was unresolved"]},{"year":2016,"claim":"Studies of the C. elegans ortholog FARL-11 demonstrated that STRIP1-family proteins localize to the ER and are required for cell-cycle-dependent ER remodeling and receptor trafficking, extending STRIP1 function beyond the cytoskeleton.","evidence":"Fluorescence localization, RNAi, live ER imaging, and GLP-1/Notch receptor localization in C. elegans embryos and germline","pmids":["27510976"],"confidence":"Medium","gaps":["Whether mammalian STRIP1 similarly localizes to ER was not shown","Mechanism linking STRIPAK to ER membrane dynamics was not defined"]},{"year":2017,"claim":"Mouse Strip1 knockout proved essential for mesoderm cell migration and embryonic axial extension, confirming a cell-autonomous requirement for STRIP1 in focal adhesion organization and migration in vivo.","evidence":"Mouse knockout, cultured mesoderm explants, MEFs, live imaging, focal adhesion and actin immunofluorescence","pmids":["29203676"],"confidence":"High","gaps":["Specific STRIP1-dependent signaling pathway(s) driving the embryonic phenotype were not fully delineated","Tissue-specific conditional knockouts were not reported"]},{"year":2018,"claim":"STRIP1 was shown to interact with CCM3 and regulate endothelial contractility upstream of Rho-ROCK signaling, connecting STRIPAK to cerebral cavernous malformation biology.","evidence":"Co-immunoprecipitation, RNAi, in vitro angiogenesis assay, ROCK inhibitor rescue in endothelial cells","pmids":["30509168"],"confidence":"Medium","gaps":["Whether STRIP1 loss contributes to CCM pathology in vivo was untested","Distinction between STRIP1 and STRIP2 contributions in endothelium was limited"]},{"year":2019,"claim":"Crystallographic analysis revealed STRIP1 as a structural arm that loads MST2 onto the STRIPAK complex in a phosphorylation-dependent, cell-density-responsive manner, providing the first structural mechanism for Hippo pathway regulation by STRIPAK.","evidence":"Crystallography, biochemical reconstitution, co-immunoprecipitation, cell-density dissociation assays, interface mutagenesis","pmids":["30622739"],"confidence":"High","gaps":["Full atomic-resolution structure of the complete STRIPAK holo-complex was lacking","Identity of the upstream signal triggering STRIP1 arm dissociation was unknown"]},{"year":2020,"claim":"Epistasis experiments demonstrated that STRIP1 loss causes cell cycle arrest through MST3/4-dependent upregulation of p21 and p27, establishing a proliferation-control axis downstream of STRIPAK.","evidence":"siRNA knockdown, flow cytometry, single-cell immunofluorescence for p21 and γH2AX, double-knockdown rescue in breast cancer cells","pmids":["32258031"],"confidence":"Medium","gaps":["Whether cell cycle arrest reflects a direct MST3/4 substrate or an indirect DNA damage response was unresolved","Single-lab finding in one cell line"]},{"year":2021,"claim":"A 3.2-Å cryo-EM structure of the STRIPAK core revealed the noncanonical PP2A architecture with a STRN3 homotetramer scaffold and identified IP6 as a structural cofactor buried within STRIP1, establishing the molecular basis for complex integrity and Hippo regulation.","evidence":"Cryo-EM structure determination, interface mutagenesis, Hippo pathway reporter assays","pmids":["33633399"],"confidence":"High","gaps":["How IP6 incorporation is regulated was not addressed","Structure did not include the kinase-loading arms in their MST-bound state"]},{"year":2022,"claim":"In vivo genetic epistasis in zebrafish showed that Strip1-Strn3 interaction within STRIPAK suppresses Jun-mediated apoptosis in retinal ganglion cells, revealing a pro-survival function in neural circuit formation.","evidence":"Zebrafish loss-of-function genetics, co-immunoprecipitation, Jun morpholino rescue of RGC survival","pmids":["35314028"],"confidence":"High","gaps":["How STRIPAK-mediated kinase regulation connects to Jun transcriptional activation was not defined","Whether this pathway operates in mammalian retina was untested"]},{"year":2023,"claim":"C. elegans studies demonstrated that the STRIP1 ortholog FARL-11 and striatin localize to the sarcoplasmic reticulum in muscle and are required for SR organization and normal levels of the Ca²⁺ release channel UNC-68, extending STRIPAK function to SR membrane architecture.","evidence":"Co-immunoprecipitation, immunofluorescence, missense mutant characterization, immunoblot in C. elegans muscle","pmids":["37314837"],"confidence":"Medium","gaps":["Whether mammalian STRIP1 plays a similar role in cardiac SR was not established","Mechanism by which STRIPAK regulates UNC-68/RyR levels was not identified"]},{"year":2026,"claim":"Strip1 was found to localize to the nucleolus in cardiomyocytes and to suppress hypertrophy by restraining MST1/2, MST4, and Calcineurin/NFAT signaling, with Strip1 reduction causing impaired cardiac function in zebrafish.","evidence":"siRNA in neonatal rat ventricular cardiomyocytes, immunofluorescence, zebrafish morpholino, kinase and NFAT reporter assays","pmids":["41892331"],"confidence":"Medium","gaps":["Nucleolar localization of STRIP1 in cardiomyocytes has not been independently confirmed","Mechanism linking STRIPAK to calcineurin/NFAT is not molecularly defined","In vivo cardiac-specific knockout data in mammals are lacking"]},{"year":null,"claim":"Key unresolved questions include the upstream signal(s) that trigger cell-density-dependent STRIP1 dissociation from STRIPAK, the direct substrates of STRIP1-regulated PP2A activity, the structural basis of the complete kinase-loaded STRIPAK holo-complex, and whether STRIP1 loss is causative for any human Mendelian disease.","evidence":"","pmids":[],"confidence":"High","gaps":["No direct PP2A substrates mediated by STRIP1 have been identified","Full holo-complex structure with kinase arms unresolved","No human disease causally linked to STRIP1 mutations"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[3,6,7,12]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[6,8]}],"localization":[{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[10,11]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0,3]},{"term_id":"GO:0005730","term_label":"nucleolus","supporting_discovery_ids":[12]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[3,6,8,9]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[7]},{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[9]}],"complexes":["STRIPAK"],"partners":["STRN3","PP2AA","PP2AC","MOB4","CCM3","MST3","MST4","MST2"],"other_free_text":[]},"mechanistic_narrative":"STRIP1 is a core structural subunit of the STRIPAK complex — a noncanonical PP2A holoenzyme built on a homotetrameric striatin scaffold — that negatively regulates MST-family kinases to control actomyosin contractility, cell migration, cell survival, and ER/SR organization across metazoan tissues. Cryo-EM and crystallographic studies show STRIP1 forms one of two arms of the STRIPAK assembly, uses inositol hexakisphosphate (IP6) as a structural cofactor, and undergoes cell-density-dependent dissociation that gates Hippo pathway activation [PMID:30622739, PMID:33633399]. By restraining MST3/4 kinase activity, STRIP1 prevents aberrant phosphorylation of PPP1R14A-D, thereby controlling the balance between cortical and focal-adhesion-based contractility that dictates cell migration mode and metastatic behavior [PMID:25531779, PMID:29203676]. STRIP1 also suppresses Jun-mediated apoptosis in retinal ganglion cells, regulates ER morphology and receptor trafficking, and restrains calcineurin/NFAT pro-hypertrophic signaling in cardiomyocytes [PMID:35314028, PMID:27510976, PMID:41892331]."},"prefetch_data":{"uniprot":{"accession":"Q5VSL9","full_name":"Striatin-interacting protein 1","aliases":["Protein FAM40A"],"length_aa":837,"mass_kda":95.6,"function":"Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/Q5VSL9/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/STRIP1","classification":"Not Classified","n_dependent_lines":502,"n_total_lines":1208,"dependency_fraction":0.4155629139072848},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MAP4K4","stoichiometry":4.0},{"gene":"CTTN","stoichiometry":0.2},{"gene":"DYNLL1","stoichiometry":0.2},{"gene":"DYNLL2","stoichiometry":0.2},{"gene":"PPP2CA","stoichiometry":0.2},{"gene":"PPP2CB","stoichiometry":0.2},{"gene":"STK24","stoichiometry":0.2},{"gene":"STK25","stoichiometry":0.2},{"gene":"STK26","stoichiometry":0.2},{"gene":"STRN3","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/STRIP1","total_profiled":1310},"omim":[{"mim_id":"617919","title":"STRIATIN-INTERACTING PROTEIN 2; STRIP2","url":"https://www.omim.org/entry/617919"},{"mim_id":"617918","title":"STRIATIN-INTERACTING PROTEIN 1; STRIP1","url":"https://www.omim.org/entry/617918"},{"mim_id":"614766","title":"STRIATIN, CALMODULIN-BINDING PROTEIN 3; STRN3","url":"https://www.omim.org/entry/614766"},{"mim_id":"610742","title":"MOV10 RISC COMPLEX RNA HELICASE; MOV10","url":"https://www.omim.org/entry/610742"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Cytosol","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/STRIP1"},"hgnc":{"alias_symbol":["FLJ14743","KIAA1761","FAR11A"],"prev_symbol":["FAM40A"]},"alphafold":{"accession":"Q5VSL9","domains":[{"cath_id":"-","chopping":"77-309_503-741","consensus_level":"medium","plddt":93.5171,"start":77,"end":741},{"cath_id":"-","chopping":"429-472","consensus_level":"medium","plddt":89.2457,"start":429,"end":472},{"cath_id":"-","chopping":"797-833","consensus_level":"medium","plddt":78.9232,"start":797,"end":833}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5VSL9","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q5VSL9-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q5VSL9-F1-predicted_aligned_error_v6.png","plddt_mean":80.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=STRIP1","jax_strain_url":"https://www.jax.org/strain/search?query=STRIP1"},"sequence":{"accession":"Q5VSL9","fasta_url":"https://rest.uniprot.org/uniprotkb/Q5VSL9.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q5VSL9/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5VSL9"}},"corpus_meta":[{"pmid":"18782753","id":"PMC_18782753","title":"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein.","date":"2008","source":"Molecular & cellular proteomics : MCP","url":"https://pubmed.ncbi.nlm.nih.gov/18782753","citation_count":301,"is_preprint":false},{"pmid":"24333164","id":"PMC_24333164","title":"STRIPAK complexes: structure, biological function, and involvement in human diseases.","date":"2013","source":"The international journal of biochemistry & cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/24333164","citation_count":183,"is_preprint":false},{"pmid":"21834987","id":"PMC_21834987","title":"Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration.","date":"2011","source":"BMC 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biology","url":"https://pubmed.ncbi.nlm.nih.gov/40924252","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":13606,"output_tokens":3214,"usd":0.044514},"stage2":{"model":"claude-opus-4-6","input_tokens":6594,"output_tokens":3190,"usd":0.16908},"total_usd":0.213594,"stage1_batch_id":"msgbatch_01RPbVc9PDH9zQmYK5Hs6srm","stage2_batch_id":"msgbatch_01JVbVLzeKN2yVrsGp3zC8aM","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2008,\n      \"finding\": \"STRIP1 (formerly FAM40A) is a novel component of the STRIPAK complex, a large multiprotein assembly containing PP2A catalytic and scaffolding subunits, striatins (PP2A regulatory B''' subunits), Mob3, STRIP2, CCM3, and germinal center kinase III family kinases; STRIPAK establishes mutually exclusive interactions with either CTTNBP2 proteins or a subcomplex of SLMAP/SIKE/FGFR1OP2.\",\n      \"method\": \"Iterative affinity purification/mass spectrometry (AP-MS) interaction network mapping\",\n      \"journal\": \"Molecular & cellular proteomics : MCP\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — large-scale AP-MS with reciprocal validation, foundational discovery replicated widely\",\n      \"pmids\": [\"18782753\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"FAM40A (STRIP1) depletion reduces cell spreading, whereas FAM40B (STRIP2) depletion induces cell elongation and tail retraction defects, identifying STRIP1 as a regulator of cell morphology and cytoskeletal organization distinct from its paralog.\",\n      \"method\": \"Genome-wide RNAi screen in Drosophila cells followed by siRNA knockdown in human cells with morphological phenotyping and actin filament imaging\",\n      \"journal\": \"BMC biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — clean KD with defined cellular phenotype, but single lab\",\n      \"pmids\": [\"21834987\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Yeast Far11, the ortholog of mammalian STRIP1/FAM40A, genetically antagonizes TORC2 signaling; Far11 interacts with PP2A subunits Tpd3 and Pph21, and deletion of Far11 restores phosphorylation of the TORC2 substrate Slm1 in tor2-21 mutants, placing the PP2A-Far11 complex as a negative regulator of TORC2.\",\n      \"method\": \"Genetic suppressor screen, co-immunoprecipitation, phosphorylation assays in Saccharomyces cerevisiae\",\n      \"journal\": \"Genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — epistasis and biochemical interaction in yeast ortholog, single lab\",\n      \"pmids\": [\"22298706\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"FAM40A (STRIP1) negatively regulates the MST3 and MST4 kinases within the STRIPAK complex; loss of FAM40A results in co-localization of contractile actomyosin machinery with ERM proteins via MST3/4-mediated phosphorylation of PPP1R14A-D (inhibitors of PPP1CB), thereby controlling the mode of cancer cell migration.\",\n      \"method\": \"siRNA knockdown, in vitro kinase assays, computational modeling, in vitro migration assays, in vivo breast cancer metastasis assays; FAM40B tumor-derived mutations shown to uncouple it from PP2A\",\n      \"journal\": \"Nature cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — multiple orthogonal methods including in vivo metastasis, kinase assays, and mutagenesis; high citation count\",\n      \"pmids\": [\"25531779\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Strip1 is essential for mesoderm cell migration in vivo; Strip1-null mouse embryos show defects in mesoderm organization and axial extension correlated with decreased cell spreading, abnormal focal adhesions, disorganized actin cytoskeleton, and decreased migration velocity in cultured mesoderm explants and MEFs.\",\n      \"method\": \"Mouse knockout, cultured mesoderm explants, mouse embryonic fibroblasts, live imaging, immunofluorescence for focal adhesions and actin\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — clean KO with defined in vivo and ex vivo cellular phenotypes, multiple orthogonal readouts\",\n      \"pmids\": [\"29203676\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"FAM40A and FAM40B interact with CCM3 and regulate endothelial cell contractility; knockdown of FAM40A or FAM40B increases stress fibers and reduces angiogenic loop formation, phenotypes that are rescued by ROCK inhibition, placing FAM40A/B upstream of Rho-ROCK signaling in endothelial cells.\",\n      \"method\": \"Co-immunoprecipitation, RNAi knockdown, in vitro angiogenesis assay, pharmacological ROCK inhibition rescue\",\n      \"journal\": \"BMC cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 — Co-IP plus functional rescue, single lab\",\n      \"pmids\": [\"30509168\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"STRIP1 forms one of two 'arms' in the STRIPAK complex that loads MST2 onto the complex in a phosphorylation-dependent manner; decreased cell density triggers dissociation of the STRIP1 arm from STRIPAK, reflecting dynamic assembly upon upstream signal sensing, while disrupting this interface abrogates STRIPAK's regulatory effect on Hippo signaling.\",\n      \"method\": \"Crystallography, biochemical reconstitution, co-immunoprecipitation, cell density-dependent dissociation assays, mutagenesis of interface residues\",\n      \"journal\": \"Cell discovery\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — crystallographic structure plus biochemical reconstitution and functional mutagenesis\",\n      \"pmids\": [\"30622739\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Loss of STRIP1 in breast cancer cells causes cell cycle arrest via induction of CDK inhibitors p21 and p27; the p21/γH2AX ratio imbalance caused by STRIP1 loss can be rescued by co-depletion of MST3 and MST4 kinases, placing STRIP1 upstream of MST3/4 in controlling p21-mediated cell cycle exit.\",\n      \"method\": \"siRNA knockdown, flow cytometry, single-cell immunofluorescence for p21 and γH2AX, epistasis by double knockdown\",\n      \"journal\": \"Frontiers in cell and developmental biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — epistasis by double KD with quantitative single-cell readouts, single lab\",\n      \"pmids\": [\"32258031\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Cryo-EM structure of the human STRIPAK core (PP2AA, PP2AC, STRN3, STRIP1, MOB4) at 3.2-Å resolution reveals a noncanonical PP2A assembly with four copies of STRN3 forming an elongated homotetrameric scaffold; an inositol hexakisphosphate (IP6) is a structural cofactor of STRIP1; mutations at subunit interfaces disrupt complex integrity and cause aberrant Hippo pathway activation.\",\n      \"method\": \"Cryo-EM structure determination, mutagenesis of interface residues, Hippo pathway reporter assays\",\n      \"journal\": \"Nature structural & molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — high-resolution cryo-EM structure with mutagenesis and functional validation\",\n      \"pmids\": [\"33633399\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Zebrafish Strip1 physically interacts with Striatin 3 (Strn3) within STRIPAK and is required for retinal ganglion cell (RGC) survival; loss of Strip1 or Strn3 activates the pro-apoptotic transcription factor Jun in RGCs, and Jun knockdown rescues RGC survival in strip1 mutants, placing Strip1 upstream of Jun-mediated apoptosis in inner retinal circuit formation.\",\n      \"method\": \"Zebrafish loss-of-function genetics, co-immunoprecipitation, immunofluorescence, epistasis by morpholino-mediated Jun knockdown\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — in vivo genetic epistasis with biochemical interaction, multiple orthogonal methods\",\n      \"pmids\": [\"35314028\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"C. elegans FARL-11 (STRIP1/2 ortholog) and CASH-1 (striatin) form a complex in vivo, both localize to the sarcoplasmic reticulum (SR) in muscle, and missense mutations in farl-11 or cash-1 disrupt SR organization around M-lines and alter levels of the SR Ca2+ release channel UNC-68, demonstrating a role for the STRIPAK complex in SR/ER organization.\",\n      \"method\": \"Co-immunoprecipitation, immunofluorescence localization, missense mutant characterization, immunoblot for UNC-68 levels in C. elegans\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct localization with functional consequence, in vivo complex formation, ortholog system\",\n      \"pmids\": [\"37314837\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"C. elegans FARL-11 (STRIP1/2 ortholog) localizes to the ER and is required for cell cycle-dependent ER morphological changes in embryos and for proper membrane localization of the GLP-1/Notch receptor in the germline, linking STRIPAK to ER dynamics and receptor trafficking.\",\n      \"method\": \"Fluorescence localization, RNAi/genetic loss-of-function, live imaging of ER morphology, GLP-1 receptor localization assay in C. elegans\",\n      \"journal\": \"Development (Cambridge, England)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct localization tied to functional consequence, ortholog system\",\n      \"pmids\": [\"27510976\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"Strip1 localizes to the nucleolus in neonatal rat ventricular cardiomyocytes and associates with cardiac STRIPAK complex; Strip1 knockdown induces cardiomyocyte hypertrophy and activates MST1/MST2 and MST4 kinases as well as Calcineurin/NFAT pro-hypertrophic signaling; morpholino-driven Strip1 reduction in zebrafish causes impaired cardiac function.\",\n      \"method\": \"siRNA knockdown in NRVCMs, immunofluorescence localization, zebrafish morpholino knockdown, kinase activity assays, NFAT reporter assays\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods, in vitro and in vivo, single lab\",\n      \"pmids\": [\"41892331\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"STRIP1 is a core structural component of the STRIPAK complex — a noncanonical PP2A holoenzyme in which STRIP1 forms one of two arms anchoring MST-family kinases to a homotetrameric STRN3 scaffold (with IP6 as a STRIP1 cofactor) — and acts as a negative regulator of MST3/4 kinase activity, thereby controlling actomyosin contractility, cell migration, ER/SR organization, and Hippo/Hippo-adjacent (Jun, Calcineurin/NFAT) pro-apoptotic and pro-hypertrophic signaling in a context-dependent, cell-density-responsive manner.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"STRIP1 is a core structural subunit of the STRIPAK complex — a noncanonical PP2A holoenzyme built on a homotetrameric striatin scaffold — that negatively regulates MST-family kinases to control actomyosin contractility, cell migration, cell survival, and ER/SR organization across metazoan tissues. Cryo-EM and crystallographic studies show STRIP1 forms one of two arms of the STRIPAK assembly, uses inositol hexakisphosphate (IP6) as a structural cofactor, and undergoes cell-density-dependent dissociation that gates Hippo pathway activation [PMID:30622739, PMID:33633399]. By restraining MST3/4 kinase activity, STRIP1 prevents aberrant phosphorylation of PPP1R14A-D, thereby controlling the balance between cortical and focal-adhesion-based contractility that dictates cell migration mode and metastatic behavior [PMID:25531779, PMID:29203676]. STRIP1 also suppresses Jun-mediated apoptosis in retinal ganglion cells, regulates ER morphology and receptor trafficking, and restrains calcineurin/NFAT pro-hypertrophic signaling in cardiomyocytes [PMID:35314028, PMID:27510976, PMID:41892331].\",\n  \"teleology\": [\n    {\n      \"year\": 2008,\n      \"claim\": \"Identification of STRIP1 as a novel STRIPAK subunit resolved the composition of a previously uncharacterized PP2A-striatin supercomplex and revealed mutually exclusive sub-assemblies within it.\",\n      \"evidence\": \"Iterative AP-MS with reciprocal bait validations in mammalian cells\",\n      \"pmids\": [\"18782753\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Functional role of STRIP1 within the complex was unknown\", \"Stoichiometry and architecture of the complex were unresolved\", \"No disease or organismal phenotype yet linked\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"RNAi screening established that STRIP1 and its paralog STRIP2 have non-redundant roles in cell morphology, with STRIP1 specifically required for normal cell spreading.\",\n      \"evidence\": \"Genome-wide Drosophila RNAi screen followed by human siRNA knockdown with morphological and actin cytoskeletal phenotyping\",\n      \"pmids\": [\"21834987\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular target through which STRIP1 controls spreading was not identified\", \"Single-lab finding not independently confirmed at the time\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Genetic epistasis in yeast placed the STRIP1 ortholog Far11 as a negative regulator of TORC2 signaling via PP2A, providing the first pathway-level positioning of STRIP1-family proteins.\",\n      \"evidence\": \"Suppressor screen, co-immunoprecipitation, and phosphorylation assays in S. cerevisiae\",\n      \"pmids\": [\"22298706\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether mammalian STRIP1 similarly antagonizes mTORC2 was untested\", \"Mechanism of PP2A substrate selection was unclear\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Mechanistic dissection revealed that STRIP1 restrains MST3/4 kinase activity within STRIPAK, and that its loss hyperactivates a MST3/4→PPP1R14A→actomyosin contractility axis that alters cancer cell migration mode and metastasis in vivo.\",\n      \"evidence\": \"siRNA, in vitro kinase assays, computational modeling, in vitro migration, and in vivo breast cancer metastasis assays with mutagenesis\",\n      \"pmids\": [\"25531779\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of STRIP1-mediated kinase inhibition was unknown\", \"Whether STRIP1 directly contacts MST3/4 or acts through PP2A catalytic activity was unresolved\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Studies of the C. elegans ortholog FARL-11 demonstrated that STRIP1-family proteins localize to the ER and are required for cell-cycle-dependent ER remodeling and receptor trafficking, extending STRIP1 function beyond the cytoskeleton.\",\n      \"evidence\": \"Fluorescence localization, RNAi, live ER imaging, and GLP-1/Notch receptor localization in C. elegans embryos and germline\",\n      \"pmids\": [\"27510976\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether mammalian STRIP1 similarly localizes to ER was not shown\", \"Mechanism linking STRIPAK to ER membrane dynamics was not defined\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Mouse Strip1 knockout proved essential for mesoderm cell migration and embryonic axial extension, confirming a cell-autonomous requirement for STRIP1 in focal adhesion organization and migration in vivo.\",\n      \"evidence\": \"Mouse knockout, cultured mesoderm explants, MEFs, live imaging, focal adhesion and actin immunofluorescence\",\n      \"pmids\": [\"29203676\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Specific STRIP1-dependent signaling pathway(s) driving the embryonic phenotype were not fully delineated\", \"Tissue-specific conditional knockouts were not reported\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"STRIP1 was shown to interact with CCM3 and regulate endothelial contractility upstream of Rho-ROCK signaling, connecting STRIPAK to cerebral cavernous malformation biology.\",\n      \"evidence\": \"Co-immunoprecipitation, RNAi, in vitro angiogenesis assay, ROCK inhibitor rescue in endothelial cells\",\n      \"pmids\": [\"30509168\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether STRIP1 loss contributes to CCM pathology in vivo was untested\", \"Distinction between STRIP1 and STRIP2 contributions in endothelium was limited\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Crystallographic analysis revealed STRIP1 as a structural arm that loads MST2 onto the STRIPAK complex in a phosphorylation-dependent, cell-density-responsive manner, providing the first structural mechanism for Hippo pathway regulation by STRIPAK.\",\n      \"evidence\": \"Crystallography, biochemical reconstitution, co-immunoprecipitation, cell-density dissociation assays, interface mutagenesis\",\n      \"pmids\": [\"30622739\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Full atomic-resolution structure of the complete STRIPAK holo-complex was lacking\", \"Identity of the upstream signal triggering STRIP1 arm dissociation was unknown\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Epistasis experiments demonstrated that STRIP1 loss causes cell cycle arrest through MST3/4-dependent upregulation of p21 and p27, establishing a proliferation-control axis downstream of STRIPAK.\",\n      \"evidence\": \"siRNA knockdown, flow cytometry, single-cell immunofluorescence for p21 and γH2AX, double-knockdown rescue in breast cancer cells\",\n      \"pmids\": [\"32258031\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether cell cycle arrest reflects a direct MST3/4 substrate or an indirect DNA damage response was unresolved\", \"Single-lab finding in one cell line\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"A 3.2-Å cryo-EM structure of the STRIPAK core revealed the noncanonical PP2A architecture with a STRN3 homotetramer scaffold and identified IP6 as a structural cofactor buried within STRIP1, establishing the molecular basis for complex integrity and Hippo regulation.\",\n      \"evidence\": \"Cryo-EM structure determination, interface mutagenesis, Hippo pathway reporter assays\",\n      \"pmids\": [\"33633399\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How IP6 incorporation is regulated was not addressed\", \"Structure did not include the kinase-loading arms in their MST-bound state\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"In vivo genetic epistasis in zebrafish showed that Strip1-Strn3 interaction within STRIPAK suppresses Jun-mediated apoptosis in retinal ganglion cells, revealing a pro-survival function in neural circuit formation.\",\n      \"evidence\": \"Zebrafish loss-of-function genetics, co-immunoprecipitation, Jun morpholino rescue of RGC survival\",\n      \"pmids\": [\"35314028\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How STRIPAK-mediated kinase regulation connects to Jun transcriptional activation was not defined\", \"Whether this pathway operates in mammalian retina was untested\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"C. elegans studies demonstrated that the STRIP1 ortholog FARL-11 and striatin localize to the sarcoplasmic reticulum in muscle and are required for SR organization and normal levels of the Ca²⁺ release channel UNC-68, extending STRIPAK function to SR membrane architecture.\",\n      \"evidence\": \"Co-immunoprecipitation, immunofluorescence, missense mutant characterization, immunoblot in C. elegans muscle\",\n      \"pmids\": [\"37314837\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether mammalian STRIP1 plays a similar role in cardiac SR was not established\", \"Mechanism by which STRIPAK regulates UNC-68/RyR levels was not identified\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Strip1 was found to localize to the nucleolus in cardiomyocytes and to suppress hypertrophy by restraining MST1/2, MST4, and Calcineurin/NFAT signaling, with Strip1 reduction causing impaired cardiac function in zebrafish.\",\n      \"evidence\": \"siRNA in neonatal rat ventricular cardiomyocytes, immunofluorescence, zebrafish morpholino, kinase and NFAT reporter assays\",\n      \"pmids\": [\"41892331\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Nucleolar localization of STRIP1 in cardiomyocytes has not been independently confirmed\", \"Mechanism linking STRIPAK to calcineurin/NFAT is not molecularly defined\", \"In vivo cardiac-specific knockout data in mammals are lacking\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Key unresolved questions include the upstream signal(s) that trigger cell-density-dependent STRIP1 dissociation from STRIPAK, the direct substrates of STRIP1-regulated PP2A activity, the structural basis of the complete kinase-loaded STRIPAK holo-complex, and whether STRIP1 loss is causative for any human Mendelian disease.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No direct PP2A substrates mediated by STRIP1 have been identified\", \"Full holo-complex structure with kinase arms unresolved\", \"No human disease causally linked to STRIP1 mutations\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [3, 6, 7, 12]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [6, 8]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [10, 11]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0005730\", \"supporting_discovery_ids\": [12]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [3, 6, 8, 9]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [7]},\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [9]}\n    ],\n    \"complexes\": [\"STRIPAK\"],\n    \"partners\": [\"STRN3\", \"PP2AA\", \"PP2AC\", \"MOB4\", \"CCM3\", \"MST3\", \"MST4\", \"MST2\"],\n    \"other_free_text\": []\n  }\n}\n```"}