{"gene":"PPP6R2","run_date":"2026-06-10T06:43:35","timeline":{"discoveries":[{"year":2024,"finding":"PPP6R2 (as part of the PP6 holoenzyme) promotes RIPK1-dependent PANoptosis downstream of TAK1 inhibition. The PP6 regulatory subunits PPP6R1, PPP6R2, and PPP6R3 have redundant roles; combined depletion of all three was required to block TAK1 inhibitor-induced cell death. Mechanistically, PPP6R2-containing PP6 complex promotes pro-death S166 auto-phosphorylation of RIPK1 and reduces pro-survival S321 phosphorylation of RIPK1.","method":"Cell death-based CRISPR screen, genetic loss-of-function (individual and combined depletion of PP6 subunits), phosphorylation analysis of RIPK1 at S166 and S321","journal":"BMC biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean CRISPR KO with defined cellular phenotype and phosphorylation readout, single lab, two orthogonal methods (screen + targeted KO + phospho-analysis)","pmids":["38807188"],"is_preprint":false},{"year":2013,"finding":"Silencing of PPP6R2 in HT-29 human colorectal cancer cells increased adhesion to liver sinusoidal endothelial cells (LSEC) and hepatic microvascular retention, identifying PPP6R2 as an anti-adhesive gene in the context of hepatic microvascular adhesion.","method":"Random homozygous gene perturbation (RHGP) screen in HT-29 cells with LSEC adhesion assay; PPP6R2 was identified in silenced state in nonadherent cells, and its silencing increased LSEC adhesion and hepatic microvascular retention","journal":"International journal of cancer","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single screening method, functional consequence identified but no molecular mechanism or pathway placement established","pmids":["23629598"],"is_preprint":false},{"year":2025,"finding":"PPP6R2 was identified as a high-confidence interactor of the CC2D1A scaffold protein in mouse hippocampus, suggesting PPP6R2 participates in a postsynaptic protein complex in neurons.","method":"Co-immunoprecipitation/mass spectrometry proteomic interactome analysis in mouse hippocampus using CC2D1A antibody, validated with Cc2d1a hypomorph mouse line controls","journal":"bioRxiv","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single Co-IP/MS experiment, preprint, no direct functional validation of PPP6R2 interaction consequence","pmids":["40667103"],"is_preprint":true}],"current_model":"PPP6R2 is a regulatory subunit of the protein phosphatase 6 (PP6) holoenzyme that, together with redundant paralogous subunits PPP6R1 and PPP6R3, promotes RIPK1-dependent PANoptosis by supporting pro-death S166 auto-phosphorylation and suppressing pro-survival S321 phosphorylation of RIPK1 downstream of TAK1 inhibition; it has also been identified as an anti-adhesive factor in colon cancer hepatic metastasis and as a putative postsynaptic interactor of the CC2D1A scaffold in neurons."},"narrative":{"mechanistic_narrative":"PPP6R2 is a regulatory subunit of the protein phosphatase 6 (PP6) holoenzyme that controls RIPK1-dependent programmed cell death [PMID:38807188]. Acting redundantly with its paralogous subunits PPP6R1 and PPP6R3, PPP6R2-containing PP6 promotes PANoptosis downstream of TAK1 inhibition, and only combined depletion of all three regulatory subunits blocks TAK1 inhibitor-induced death [PMID:38807188]. Mechanistically, the complex tips RIPK1 toward a pro-death state by supporting auto-phosphorylation at S166 while reducing the pro-survival S321 phosphorylation [PMID:38807188]. Beyond this role in cell-death signaling, the broader cellular functions of PPP6R2 have not been characterized in the available corpus.","teleology":[{"year":2013,"claim":"Before any signaling role was known, a screen asked whether PPP6R2 influences cancer cell adhesion, establishing it as a functional modifier of hepatic microvascular retention.","evidence":"Random homozygous gene perturbation screen in HT-29 colorectal cancer cells with liver sinusoidal endothelial cell adhesion assay","pmids":["23629598"],"confidence":"Low","gaps":["No molecular mechanism or pathway placement established for the anti-adhesive phenotype","Effect of PP6 catalytic activity on adhesion not tested","Not connected to any defined phosphorylation substrate"]},{"year":2024,"claim":"It was unknown how PP6 regulatory subunits gate RIPK1-driven death; this work showed PPP6R2 acts redundantly within PP6 to promote pro-death RIPK1 S166 auto-phosphorylation and suppress pro-survival S321 phosphorylation downstream of TAK1 inhibition.","evidence":"Cell death-based CRISPR screen with individual and combined loss-of-function of PP6 subunits and RIPK1 phospho-site analysis","pmids":["38807188"],"confidence":"Medium","gaps":["Redundancy of PPP6R1/R2/R3 leaves the unique contribution of PPP6R2 undefined","Direct dephosphorylation of RIPK1 S321 by PP6 not demonstrated biochemically","Structural basis for substrate targeting not resolved"]},{"year":2025,"claim":"Whether PPP6R2 operates outside immune/death signaling was open; an interactome placed it within a postsynaptic CC2D1A-associated complex in neurons.","evidence":"Co-immunoprecipitation/mass spectrometry of CC2D1A in mouse hippocampus with Cc2d1a hypomorph controls (preprint)","pmids":["40667103"],"confidence":"Low","gaps":["Single Co-IP/MS without reciprocal validation or functional consequence","Direct versus indirect nature of the CC2D1A association unresolved","No demonstration of PP6 phosphatase activity at the synapse"]},{"year":null,"claim":"How PPP6R2 confers substrate specificity to PP6 and whether its adhesion, death-signaling, and neuronal interactions reflect one shared biochemical activity remains unresolved.","evidence":"No timeline finding unifies the cellular contexts or defines a PPP6R2-specific substrate repertoire","pmids":[],"confidence":"Low","gaps":["No PPP6R2-specific (non-redundant) substrate identified","No structural model of the PPP6R2-containing holoenzyme","Mechanism linking PP6 activity to adhesion and synaptic biology unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0]}],"localization":[],"pathway":[{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[0]}],"complexes":["protein phosphatase 6 (PP6) holoenzyme"],"partners":["RIPK1","PPP6R1","PPP6R3","CC2D1A"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O75170","full_name":"Serine/threonine-protein phosphatase 6 regulatory subunit 2","aliases":["SAPS domain family member 2"],"length_aa":966,"mass_kda":104.9,"function":"Regulatory subunit of protein phosphatase 6 (PP6). May function as a scaffolding PP6 subunit. Involved in the PP6-mediated dephosphorylation of NFKBIE opposing its degradation in response to TNF","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/O75170/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/PPP6R2","classification":"Not Classified","n_dependent_lines":53,"n_total_lines":1208,"dependency_fraction":0.043874172185430466},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"ANKRD28","stoichiometry":10.0},{"gene":"ANKRD52","stoichiometry":4.0}],"url":"https://opencell.sf.czbiohub.org/search/PPP6R2","total_profiled":1310},"omim":[{"mim_id":"610877","title":"PROTEIN PHOSPHATASE 6, REGULATORY SUBUNIT 2; 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all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/PPP6R2"},"hgnc":{"alias_symbol":["dJ579N16.1","SAP190"],"prev_symbol":["KIAA0685","SAPS2"]},"alphafold":{"accession":"O75170","domains":[{"cath_id":"-","chopping":"440-532","consensus_level":"medium","plddt":91.2794,"start":440,"end":532},{"cath_id":"1.25.40","chopping":"12-190","consensus_level":"medium","plddt":94.0463,"start":12,"end":190}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O75170","model_url":"https://alphafold.ebi.ac.uk/files/AF-O75170-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O75170-F1-predicted_aligned_error_v6.png","plddt_mean":64.62},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=PPP6R2","jax_strain_url":"https://www.jax.org/strain/search?query=PPP6R2"},"sequence":{"accession":"O75170","fasta_url":"https://rest.uniprot.org/uniprotkb/O75170.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O75170/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O75170"}},"corpus_meta":[{"pmid":"38155330","id":"PMC_38155330","title":"Multi-ancestry 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The PP6 regulatory subunits PPP6R1, PPP6R2, and PPP6R3 have redundant roles; combined depletion of all three was required to block TAK1 inhibitor-induced cell death. Mechanistically, PPP6R2-containing PP6 complex promotes pro-death S166 auto-phosphorylation of RIPK1 and reduces pro-survival S321 phosphorylation of RIPK1.\",\n      \"method\": \"Cell death-based CRISPR screen, genetic loss-of-function (individual and combined depletion of PP6 subunits), phosphorylation analysis of RIPK1 at S166 and S321\",\n      \"journal\": \"BMC biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean CRISPR KO with defined cellular phenotype and phosphorylation readout, single lab, two orthogonal methods (screen + targeted KO + phospho-analysis)\",\n      \"pmids\": [\"38807188\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Silencing of PPP6R2 in HT-29 human colorectal cancer cells increased adhesion to liver sinusoidal endothelial cells (LSEC) and hepatic microvascular retention, identifying PPP6R2 as an anti-adhesive gene in the context of hepatic microvascular adhesion.\",\n      \"method\": \"Random homozygous gene perturbation (RHGP) screen in HT-29 cells with LSEC adhesion assay; PPP6R2 was identified in silenced state in nonadherent cells, and its silencing increased LSEC adhesion and hepatic microvascular retention\",\n      \"journal\": \"International journal of cancer\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single screening method, functional consequence identified but no molecular mechanism or pathway placement established\",\n      \"pmids\": [\"23629598\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"PPP6R2 was identified as a high-confidence interactor of the CC2D1A scaffold protein in mouse hippocampus, suggesting PPP6R2 participates in a postsynaptic protein complex in neurons.\",\n      \"method\": \"Co-immunoprecipitation/mass spectrometry proteomic interactome analysis in mouse hippocampus using CC2D1A antibody, validated with Cc2d1a hypomorph mouse line controls\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single Co-IP/MS experiment, preprint, no direct functional validation of PPP6R2 interaction consequence\",\n      \"pmids\": [\"40667103\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"PPP6R2 is a regulatory subunit of the protein phosphatase 6 (PP6) holoenzyme that, together with redundant paralogous subunits PPP6R1 and PPP6R3, promotes RIPK1-dependent PANoptosis by supporting pro-death S166 auto-phosphorylation and suppressing pro-survival S321 phosphorylation of RIPK1 downstream of TAK1 inhibition; it has also been identified as an anti-adhesive factor in colon cancer hepatic metastasis and as a putative postsynaptic interactor of the CC2D1A scaffold in neurons.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PPP6R2 is a regulatory subunit of the protein phosphatase 6 (PP6) holoenzyme that controls RIPK1-dependent programmed cell death [#0]. Acting redundantly with its paralogous subunits PPP6R1 and PPP6R3, PPP6R2-containing PP6 promotes PANoptosis downstream of TAK1 inhibition, and only combined depletion of all three regulatory subunits blocks TAK1 inhibitor-induced death [#0]. Mechanistically, the complex tips RIPK1 toward a pro-death state by supporting auto-phosphorylation at S166 while reducing the pro-survival S321 phosphorylation [#0]. Beyond this role in cell-death signaling, the broader cellular functions of PPP6R2 have not been characterized in the available corpus.\"\n,\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Before any signaling role was known, a screen asked whether PPP6R2 influences cancer cell adhesion, establishing it as a functional modifier of hepatic microvascular retention.\",\n      \"evidence\": \"Random homozygous gene perturbation screen in HT-29 colorectal cancer cells with liver sinusoidal endothelial cell adhesion assay\",\n      \"pmids\": [\"23629598\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No molecular mechanism or pathway placement established for the anti-adhesive phenotype\",\n        \"Effect of PP6 catalytic activity on adhesion not tested\",\n        \"Not connected to any defined phosphorylation substrate\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"It was unknown how PP6 regulatory subunits gate RIPK1-driven death; this work showed PPP6R2 acts redundantly within PP6 to promote pro-death RIPK1 S166 auto-phosphorylation and suppress pro-survival S321 phosphorylation downstream of TAK1 inhibition.\",\n      \"evidence\": \"Cell death-based CRISPR screen with individual and combined loss-of-function of PP6 subunits and RIPK1 phospho-site analysis\",\n      \"pmids\": [\"38807188\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Redundancy of PPP6R1/R2/R3 leaves the unique contribution of PPP6R2 undefined\",\n        \"Direct dephosphorylation of RIPK1 S321 by PP6 not demonstrated biochemically\",\n        \"Structural basis for substrate targeting not resolved\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether PPP6R2 operates outside immune/death signaling was open; an interactome placed it within a postsynaptic CC2D1A-associated complex in neurons.\",\n      \"evidence\": \"Co-immunoprecipitation/mass spectrometry of CC2D1A in mouse hippocampus with Cc2d1a hypomorph controls (preprint)\",\n      \"pmids\": [\"40667103\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single Co-IP/MS without reciprocal validation or functional consequence\",\n        \"Direct versus indirect nature of the CC2D1A association unresolved\",\n        \"No demonstration of PP6 phosphatase activity at the synapse\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How PPP6R2 confers substrate specificity to PP6 and whether its adhesion, death-signaling, and neuronal interactions reflect one shared biochemical activity remains unresolved.\",\n      \"evidence\": \"No timeline finding unifies the cellular contexts or defines a PPP6R2-specific substrate repertoire\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No PPP6R2-specific (non-redundant) substrate identified\",\n        \"No structural model of the PPP6R2-containing holoenzyme\",\n        \"Mechanism linking PP6 activity to adhesion and synaptic biology unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [\"protein phosphatase 6 (PP6) holoenzyme\"],\n    \"partners\": [\"RIPK1\", \"PPP6R1\", \"PPP6R3\", \"CC2D1A\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":2,"faith_total":3,"faith_pct":66.66666666666667}}