{"gene":"MCC","run_date":"2026-06-10T02:59:50","timeline":{"discoveries":[{"year":1996,"finding":"The MCC protein is a cytoplasmic 100-kDa phosphoprotein whose phosphorylation state changes in a cell cycle-dependent manner (weakly phosphorylated in G0/G1, highly phosphorylated during G1-to-S transition). Overexpression of wild-type MCC blocked serum-induced cell cycle progression from G1 to S phase, whereas a colorectal-tumor-derived mutant MCC failed to block this transition.","method":"Specific antibody detection, immunoelectron microscopy, cell cycle synchronization with phosphorylation analysis, overexpression and cell cycle assay in NIH3T3 cells","journal":"The Journal of Biological Chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct overexpression/mutant comparison with defined phenotypic readout (G1-S block), single lab, multiple orthogonal methods","pmids":["8626604"],"is_preprint":false},{"year":1999,"finding":"MCC protein localizes on microvilli and in apical cytoplasm in epithelial cells (renal tubule, pancreatic acinar, hepatocytes), at lateral cell borders in colon epithelium, and is associated with plasma membrane and membrane organelles in neuronal cells. MCC expression increases during NGF-induced differentiation of PC12 cells, suggesting a role in cell differentiation in addition to cell cycle regulation.","method":"Immunohistochemistry and immunoelectron microscopy in mouse tissues; immunostaining of NGF-treated PC12 cells","journal":"The journal of histochemistry and cytochemistry","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization by immunoelectron microscopy in multiple tissue types with functional inference from differentiation model; single lab","pmids":["10449536"],"is_preprint":false},{"year":2009,"finding":"MCC was identified as a new binding partner for the tumor suppressor Scrib (Scribble). MCC interacts with both Scrib and the NHERF1/NHERF2/Ezrin complex in a PDZ-dependent manner. MCC and Scrib colocalize at the cell membrane. Reduced expression of MCC impairs directed cell migration in T47D epithelial cells, an effect independent of Rac1, Cdc42, and PAK activation.","method":"Yeast two-hybrid, co-immunoprecipitation, colocalization imaging, siRNA knockdown with migration assays","journal":"FEBS letters","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal interaction confirmed by multiple methods, functional knockdown with defined phenotype, single lab","pmids":["19555689"],"is_preprint":false},{"year":2012,"finding":"Serine 828 at position -1 of MCC's PDZ-binding motif (PBM) is phosphorylated in vivo. Endogenous MCC localizes at the active migratory edge of cells, where it interacts with Scrib and non-muscle Myosin-IIB. A phosphomimetic MCC-S828D mutation strongly impairs lamellipodia formation and causes accumulation of Myosin-IIB in the membrane cortex fraction, indicating that phosphorylation of the PBM regulates MCC-Scrib-Myosin-IIB complex function in lamellipodia formation.","method":"Phosphorylation site identification, phosphomimetic and phosphodeficient mutagenesis, co-immunoprecipitation, subcellular fractionation, lamellipodia formation assays","journal":"Biochimica et biophysica acta","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — phosphorylation site mapped with functional mutagenesis and defined cellular phenotype, single lab","pmids":["22480440"],"is_preprint":false},{"year":2014,"finding":"MCC interacts with the beta-catenin repressor DBC1 (Deleted in Breast Cancer 1). MCC overexpression relocalizes DBC1 from the nucleus to the cytoplasm, reducing beta-catenin K49 acetylation via a mechanism involving SIRT1. RNAi of DBC1 promotes beta-catenin transcriptional activity, and DBC1 is required for MCC-mediated beta-catenin repression. MCC binds a glutamic-acid-rich region of DBC1 (distinct from the DBC1 Leucine Zipper domain used by all other known DBC1 partners). A disease-associated MCC mutation strongly impairs this beta-catenin repressor function.","method":"Co-immunoprecipitation, RNA interference, overexpression, subcellular fractionation, reporter assays, acetylation assays, pharmacological SIRT1 inhibition","journal":"International journal of cancer","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (Co-IP, RNAi, localization, enzymatic assay), single lab","pmids":["24824780"],"is_preprint":false},{"year":2014,"finding":"MCC is a PDZ domain-containing protein required for non-canonical Wnt5b/Vangl2/Ror2 signaling during convergence and extension (CE) in zebrafish gastrulation. Knockdown of mcc produces CE defects similar to loss of vangl2 or wnt5b. Mcc overexpression rescues depletion of wnt5b, vangl2, and ror2. Direct physical interaction between Mcc and the Vangl2 cytoplasmic tail was established biochemically. CE defects in mcc morphants are suppressed by downstream activation of RhoA and JNK, placing Mcc upstream of RhoA/JNK in the Wnt/PCP pathway.","method":"Zebrafish morpholino knockdown, overexpression rescue, co-immunoprecipitation (Mcc-Vangl2 interaction), genetic epistasis (RhoA/JNK activation)","journal":"Development (Cambridge, England)","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal rescue experiments, direct biochemical interaction, epistasis with downstream effectors, multiple orthogonal methods in one study","pmids":["25183869"],"is_preprint":false},{"year":2017,"finding":"MCC knockdown in HCT116 colon cancer cells reduces E-cadherin protein level, disrupts the E-cadherin/beta-catenin complex, and impairs cell-cell adhesive strength and epithelial integrity. MCC physically interacts with the E-cadherin/beta-catenin complex (established by co-immunoprecipitation). Loss of MCC enhances hepatocyte growth factor-induced cell scatter and tumor cell invasiveness, which is abrogated by the Src/Abl inhibitor dasatinib.","method":"siRNA knockdown, co-immunoprecipitation, dispase assay, transepithelial electrical resistance, organotypic invasion assay, pharmacological rescue","journal":"Oncogene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP establishing direct protein complex, loss-of-function with multiple defined phenotypic readouts, single lab","pmids":["29035389"],"is_preprint":false},{"year":2019,"finding":"Crystal structures of the Scribble PDZ1 domain bound to the unphosphorylated MCC PDZ-binding motif (PBM) and to phosphorylated MCC (phospho-Ser at -1 position) were determined. Scribble PDZ1 and PDZ3 are the major domains interacting with the MCC PBM. Phosphorylation at the -1 Ser position of MCC has only a minor effect on binding affinity to Scribble PDZ domains; the phospho-Ser makes no major contacts with PDZ1 in the structure, suggesting phosphorylation's functional impact extends beyond simple affinity modulation.","method":"Crystal structure determination, affinity measurements (ITC or equivalent), systematic binding assays across all four Scribble PDZ domains","journal":"The FEBS journal","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structures with functional validation by affinity measurements, multiple orthogonal methods, directly testing phosphorylation impact","pmids":["31317644"],"is_preprint":false},{"year":2001,"finding":"A novel MCC paralogue, MCC2, was identified by yeast two-hybrid screening as a binding partner of the PDZ-domain protein AIE-75. MCC2 binds the first PDZ domain of AIE-75 via its C-terminal residues (-DTFL). In contrast, MCC1 (canonical MCC) does not bind AIE-75, indicating distinct interaction profiles for the two paralogues.","method":"Yeast two-hybrid screening, interaction domain mapping","journal":"Gene","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single yeast two-hybrid method, no in vivo confirmation reported, single lab","pmids":["11311560"],"is_preprint":false}],"current_model":"MCC (Mutated in Colorectal Cancer) encodes a cytoplasmic PDZ domain-containing phosphoprotein that negatively regulates cell cycle progression from G1 to S phase, interacts with the E-cadherin/β-catenin complex to maintain cell-cell adhesion, sequesters the β-catenin coactivator DBC1 in the cytoplasm to suppress β-catenin transcriptional activity via SIRT1-mediated deacetylation, and functions as an intracellular effector of non-canonical Wnt5b/Vangl2/Ror2 signaling (upstream of RhoA/JNK) during embryonic convergence and extension; its PDZ-binding motif mediates phosphorylation-regulated interactions with Scrib and Myosin-IIB to control lamellipodia formation and cell migration."},"narrative":{"mechanistic_narrative":"MCC (Mutated in Colorectal Cancer) is a cytoplasmic PDZ-binding-motif phosphoprotein that integrates cell-cycle control, cell-cell adhesion, and non-canonical Wnt signaling at epithelial membranes [PMID:8626604, PMID:25183869, PMID:29035389]. It was first defined as a 100-kDa phosphoprotein whose phosphorylation rises during the G1-to-S transition, and whose wild-type form blocks serum-induced G1-to-S progression while a colorectal-tumor-derived mutant fails to do so [PMID:8626604]. MCC localizes to apical microvilli and lateral cell borders in epithelia and concentrates at the active migratory edge of cells [PMID:10449536, PMID:22480440]. Through its C-terminal PDZ-binding motif it engages the Scribble polarity protein, and Ser828 phosphorylation at the -1 position regulates a MCC-Scribble-Myosin-IIB complex that governs lamellipodia formation and directed migration [PMID:19555689, PMID:22480440]; crystallography of Scribble PDZ1 bound to phosphorylated and unphosphorylated MCC shows the phospho-Ser makes no major PDZ contacts, indicating that phosphorylation acts beyond simple affinity tuning [PMID:31317644]. MCC restrains Wnt/β-catenin output by two routes: it physically associates with and stabilizes the E-cadherin/β-catenin adhesion complex to maintain epithelial integrity and limit HGF-induced scatter and invasion [PMID:29035389], and it sequesters the β-catenin coactivator DBC1 in the cytoplasm, reducing β-catenin K49 acetylation via SIRT1 to suppress its transcriptional activity [PMID:24824780]. In zebrafish gastrulation MCC binds the Vangl2 cytoplasmic tail and acts as an intracellular effector of Wnt5b/Vangl2/Ror2 planar cell polarity signaling upstream of RhoA/JNK during convergence and extension [PMID:25183869]. Disease-associated MCC mutations impair both its G1-to-S block and its DBC1/β-catenin repressor function [PMID:8626604, PMID:24824780].","teleology":[{"year":1996,"claim":"Established that MCC is a cell-cycle-regulated phosphoprotein that actively restrains the G1-to-S transition, and that a tumor-derived mutation abolishes this control.","evidence":"Phosphorylation analysis across synchronized cell cycle plus wild-type versus mutant overexpression in NIH3T3 cells","pmids":["8626604"],"confidence":"Medium","gaps":["The kinase phosphorylating MCC and the molecular target of its G1-S block were not identified","Endogenous loss-of-function consequence not tested"]},{"year":1999,"claim":"Defined MCC's subcellular and tissue distribution, placing it at apical/lateral epithelial membranes and linking it to differentiation beyond cell-cycle control.","evidence":"Immunohistochemistry and immunoelectron microscopy across mouse epithelia and neuronal cells, plus NGF-induced PC12 differentiation","pmids":["10449536"],"confidence":"Medium","gaps":["Membrane-targeting mechanism unknown","Functional role in differentiation inferred from expression, not perturbation"]},{"year":2009,"claim":"Identified Scribble as a PDZ-dependent MCC partner and tied MCC to directed epithelial migration, distinguishing its pathway from canonical Rac1/Cdc42/PAK signaling.","evidence":"Yeast two-hybrid, co-IP, colocalization, and siRNA migration assays in T47D cells","pmids":["19555689"],"confidence":"Medium","gaps":["Downstream effectors of the MCC-Scrib axis in migration not defined","Single cell-line context"]},{"year":2012,"claim":"Mapped Ser828 in the MCC PDZ-binding motif as a phosphorylation switch controlling a MCC-Scrib-Myosin-IIB complex governing lamellipodia formation.","evidence":"Phospho-site mapping, phosphomimetic/phosphodeficient mutagenesis, co-IP, fractionation, and lamellipodia assays","pmids":["22480440"],"confidence":"Medium","gaps":["Kinase responsible for Ser828 phosphorylation not identified","Mechanistic link between PBM phosphorylation and Myosin-IIB cortical accumulation not resolved"]},{"year":2014,"claim":"Revealed a mechanism by which MCC suppresses β-catenin transcriptional output: cytoplasmic sequestration of DBC1 leading to SIRT1-dependent β-catenin deacetylation.","evidence":"Co-IP, RNAi, fractionation, reporter and acetylation assays, and pharmacological SIRT1 inhibition","pmids":["24824780"],"confidence":"Medium","gaps":["Whether MCC directly regulates SIRT1 or acts only through DBC1 relocalization not resolved","Single-lab biochemistry"]},{"year":2014,"claim":"Placed MCC as an intracellular effector of non-canonical Wnt/PCP signaling by demonstrating direct Vangl2 binding and epistasis upstream of RhoA/JNK during convergence and extension.","evidence":"Zebrafish morpholino knockdown, reciprocal overexpression rescue, Mcc-Vangl2 co-IP, and RhoA/JNK epistasis","pmids":["25183869"],"confidence":"High","gaps":["How Mcc transduces Vangl2 engagement to RhoA/JNK activation not defined","Morpholino-based knockdown without genetic mutant confirmation"]},{"year":2017,"claim":"Showed MCC physically stabilizes the E-cadherin/β-catenin adhesion complex and that its loss licenses HGF-driven, Src/Abl-dependent invasion.","evidence":"siRNA knockdown, co-IP, dispase and TEER adhesion assays, organotypic invasion, and dasatinib rescue in HCT116 cells","pmids":["29035389"],"confidence":"Medium","gaps":["Direct versus indirect nature of the MCC-cadherin association not dissected","Mechanism by which MCC loss activates Src/Abl signaling unknown"]},{"year":2019,"claim":"Provided structural detail of the MCC-Scribble interface, showing that PBM Ser828 phosphorylation only weakly affects binding affinity, implying a regulatory function beyond simple affinity modulation.","evidence":"Crystal structures of Scribble PDZ1 with phospho- and unphospho-MCC PBM plus affinity measurements across all four Scribble PDZ domains","pmids":["31317644"],"confidence":"High","gaps":["The non-affinity mechanism by which phosphorylation alters MCC function in cells not established","Structural basis of MCC-Myosin-IIB coupling not addressed"]},{"year":null,"claim":"The kinase(s) controlling MCC's cell-cycle and PBM phosphorylation, and how its adhesion, β-catenin-repressive, and PCP functions are coordinated in a single cell, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No upstream kinase identified for any MCC phosphosite","No unified model linking G1-S control, adhesion, DBC1 sequestration, and Wnt/PCP","MCC2 paralogue function in vivo uncharacterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[2,3,5]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[4,6]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0]},{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[1,2,3]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[4,5,6]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[0]},{"term_id":"R-HSA-1500931","term_label":"Cell-Cell communication","supporting_discovery_ids":[6]}],"complexes":["MCC-Scribble-Myosin-IIB complex","E-cadherin/β-catenin complex"],"partners":["SCRIB","MYH10","CCAR2","VANGL2","CDH1","CTNNB1","NHERF1","EZR"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P23508","full_name":"Colorectal mutant cancer protein","aliases":[],"length_aa":829,"mass_kda":93.0,"function":"Candidate for the putative colorectal tumor suppressor gene located at 5q21. Suppresses cell proliferation and the Wnt/b-catenin pathway in colorectal cancer cells. Inhibits DNA binding of b-catenin/TCF/LEF transcription factors. Involved in cell migration independently of RAC1, CDC42 and p21-activated kinase (PAK) activation (PubMed:18591935, PubMed:19555689, PubMed:22480440). Represses the beta-catenin pathway (canonical Wnt signaling pathway) in a CCAR2-dependent manner by sequestering CCAR2 to the cytoplasm, thereby impairing its ability to inhibit SIRT1 which is involved in the deacetylation and negative regulation of beta-catenin (CTNB1) transcriptional activity (PubMed:24824780)","subcellular_location":"Cell membrane; Cell projection, lamellipodium; Nucleus; Cytoplasm","url":"https://www.uniprot.org/uniprotkb/P23508/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/MCC","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"CAPZB","stoichiometry":0.2},{"gene":"CSNK1A1","stoichiometry":0.2},{"gene":"CSNK1E","stoichiometry":0.2},{"gene":"RBM12","stoichiometry":0.2},{"gene":"RBM14","stoichiometry":0.2},{"gene":"SNX27","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/MCC","total_profiled":1310},"omim":[{"mim_id":"620335","title":"CELL DIVISION CYCLE 20B; CDC20B","url":"https://www.omim.org/entry/620335"},{"mim_id":"618136","title":"MAD2L1-BINDING PROTEIN; MAD2L1BP","url":"https://www.omim.org/entry/618136"},{"mim_id":"615654","title":"DEAFNESS, AUTOSOMAL DOMINANT 58; DFNA58","url":"https://www.omim.org/entry/615654"},{"mim_id":"614717","title":"ANAPHASE-PROMOTING COMPLEX, SUBUNIT 15; ANAPC15","url":"https://www.omim.org/entry/614717"},{"mim_id":"614534","title":"ANAPHASE-PROMOTING COMPLEX SUBUNIT 11; ANAPC11","url":"https://www.omim.org/entry/614534"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"ovary","ntpm":54.7}],"url":"https://www.proteinatlas.org/search/MCC"},"hgnc":{"alias_symbol":[],"prev_symbol":[]},"alphafold":{"accession":"P23508","domains":[{"cath_id":"-","chopping":"608-682_721-816","consensus_level":"medium","plddt":91.6978,"start":608,"end":816},{"cath_id":"1.20.5","chopping":"37-99","consensus_level":"medium","plddt":94.6484,"start":37,"end":99},{"cath_id":"1.20.5","chopping":"232-280","consensus_level":"medium","plddt":94.1231,"start":232,"end":280}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P23508","model_url":"https://alphafold.ebi.ac.uk/files/AF-P23508-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P23508-F1-predicted_aligned_error_v6.png","plddt_mean":74.12},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=MCC","jax_strain_url":"https://www.jax.org/strain/search?query=MCC"},"sequence":{"accession":"P23508","fasta_url":"https://rest.uniprot.org/uniprotkb/P23508.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P23508/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P23508"}},"corpus_meta":[{"pmid":"1565631","id":"PMC_1565631","title":"Loss of heterozygosity involving the APC and MCC genetic loci occurs in the majority of human esophageal cancers.","date":"1992","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/1565631","citation_count":235,"is_preprint":false},{"pmid":"1346256","id":"PMC_1346256","title":"Loss of heterozygosity affecting the p53, Rb, and mcc/apc tumor suppressor gene loci in dysplastic and cancerous ulcerative colitis.","date":"1992","source":"Cancer research","url":"https://pubmed.ncbi.nlm.nih.gov/1346256","citation_count":166,"is_preprint":false},{"pmid":"21926987","id":"PMC_21926987","title":"APC15 drives the turnover of MCC-CDC20 to make the spindle assembly checkpoint responsive to kinetochore attachment.","date":"2011","source":"Nature cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/21926987","citation_count":134,"is_preprint":false},{"pmid":"1348017","id":"PMC_1348017","title":"Polymorphic sites within the MCC and APC loci reveal very frequent loss of heterozygosity in human small cell lung cancer.","date":"1992","source":"Cancer research","url":"https://pubmed.ncbi.nlm.nih.gov/1348017","citation_count":120,"is_preprint":false},{"pmid":"23007861","id":"PMC_23007861","title":"APC15 mediates CDC20 autoubiquitylation by APC/C(MCC) and disassembly of the mitotic checkpoint complex.","date":"2012","source":"Nature structural & molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/23007861","citation_count":119,"is_preprint":false},{"pmid":"22100920","id":"PMC_22100920","title":"p31comet-mediated extraction of Mad2 from the MCC promotes efficient mitotic exit.","date":"2011","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/22100920","citation_count":115,"is_preprint":false},{"pmid":"9128249","id":"PMC_9128249","title":"Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC.","date":"1997","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/9128249","citation_count":101,"is_preprint":false},{"pmid":"18662762","id":"PMC_18662762","title":"Mono-N-carboxymethyl chitosan (MCC) and N-trimethyl chitosan (TMC) nanoparticles for non-invasive vaccine delivery.","date":"2008","source":"International journal of pharmaceutics","url":"https://pubmed.ncbi.nlm.nih.gov/18662762","citation_count":100,"is_preprint":false},{"pmid":"8318422","id":"PMC_8318422","title":"Allele loss from 5q21 (APC/MCC) and 18q21 (DCC) and DCC mRNA expression in breast cancer.","date":"1993","source":"British journal of cancer","url":"https://pubmed.ncbi.nlm.nih.gov/8318422","citation_count":94,"is_preprint":false},{"pmid":"8194705","id":"PMC_8194705","title":"Allelic deletions of MCC/APC and p53 are frequent late events in human gastric 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Overexpression of wild-type MCC blocked serum-induced cell cycle progression from G1 to S phase, whereas a colorectal-tumor-derived mutant MCC failed to block this transition.\",\n      \"method\": \"Specific antibody detection, immunoelectron microscopy, cell cycle synchronization with phosphorylation analysis, overexpression and cell cycle assay in NIH3T3 cells\",\n      \"journal\": \"The Journal of Biological Chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct overexpression/mutant comparison with defined phenotypic readout (G1-S block), single lab, multiple orthogonal methods\",\n      \"pmids\": [\"8626604\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 1999,\n      \"finding\": \"MCC protein localizes on microvilli and in apical cytoplasm in epithelial cells (renal tubule, pancreatic acinar, hepatocytes), at lateral cell borders in colon epithelium, and is associated with plasma membrane and membrane organelles in neuronal cells. MCC expression increases during NGF-induced differentiation of PC12 cells, suggesting a role in cell differentiation in addition to cell cycle regulation.\",\n      \"method\": \"Immunohistochemistry and immunoelectron microscopy in mouse tissues; immunostaining of NGF-treated PC12 cells\",\n      \"journal\": \"The journal of histochemistry and cytochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization by immunoelectron microscopy in multiple tissue types with functional inference from differentiation model; single lab\",\n      \"pmids\": [\"10449536\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"MCC was identified as a new binding partner for the tumor suppressor Scrib (Scribble). MCC interacts with both Scrib and the NHERF1/NHERF2/Ezrin complex in a PDZ-dependent manner. MCC and Scrib colocalize at the cell membrane. Reduced expression of MCC impairs directed cell migration in T47D epithelial cells, an effect independent of Rac1, Cdc42, and PAK activation.\",\n      \"method\": \"Yeast two-hybrid, co-immunoprecipitation, colocalization imaging, siRNA knockdown with migration assays\",\n      \"journal\": \"FEBS letters\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal interaction confirmed by multiple methods, functional knockdown with defined phenotype, single lab\",\n      \"pmids\": [\"19555689\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Serine 828 at position -1 of MCC's PDZ-binding motif (PBM) is phosphorylated in vivo. Endogenous MCC localizes at the active migratory edge of cells, where it interacts with Scrib and non-muscle Myosin-IIB. A phosphomimetic MCC-S828D mutation strongly impairs lamellipodia formation and causes accumulation of Myosin-IIB in the membrane cortex fraction, indicating that phosphorylation of the PBM regulates MCC-Scrib-Myosin-IIB complex function in lamellipodia formation.\",\n      \"method\": \"Phosphorylation site identification, phosphomimetic and phosphodeficient mutagenesis, co-immunoprecipitation, subcellular fractionation, lamellipodia formation assays\",\n      \"journal\": \"Biochimica et biophysica acta\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — phosphorylation site mapped with functional mutagenesis and defined cellular phenotype, single lab\",\n      \"pmids\": [\"22480440\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"MCC interacts with the beta-catenin repressor DBC1 (Deleted in Breast Cancer 1). MCC overexpression relocalizes DBC1 from the nucleus to the cytoplasm, reducing beta-catenin K49 acetylation via a mechanism involving SIRT1. RNAi of DBC1 promotes beta-catenin transcriptional activity, and DBC1 is required for MCC-mediated beta-catenin repression. MCC binds a glutamic-acid-rich region of DBC1 (distinct from the DBC1 Leucine Zipper domain used by all other known DBC1 partners). A disease-associated MCC mutation strongly impairs this beta-catenin repressor function.\",\n      \"method\": \"Co-immunoprecipitation, RNA interference, overexpression, subcellular fractionation, reporter assays, acetylation assays, pharmacological SIRT1 inhibition\",\n      \"journal\": \"International journal of cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (Co-IP, RNAi, localization, enzymatic assay), single lab\",\n      \"pmids\": [\"24824780\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"MCC is a PDZ domain-containing protein required for non-canonical Wnt5b/Vangl2/Ror2 signaling during convergence and extension (CE) in zebrafish gastrulation. Knockdown of mcc produces CE defects similar to loss of vangl2 or wnt5b. Mcc overexpression rescues depletion of wnt5b, vangl2, and ror2. Direct physical interaction between Mcc and the Vangl2 cytoplasmic tail was established biochemically. CE defects in mcc morphants are suppressed by downstream activation of RhoA and JNK, placing Mcc upstream of RhoA/JNK in the Wnt/PCP pathway.\",\n      \"method\": \"Zebrafish morpholino knockdown, overexpression rescue, co-immunoprecipitation (Mcc-Vangl2 interaction), genetic epistasis (RhoA/JNK activation)\",\n      \"journal\": \"Development (Cambridge, England)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal rescue experiments, direct biochemical interaction, epistasis with downstream effectors, multiple orthogonal methods in one study\",\n      \"pmids\": [\"25183869\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"MCC knockdown in HCT116 colon cancer cells reduces E-cadherin protein level, disrupts the E-cadherin/beta-catenin complex, and impairs cell-cell adhesive strength and epithelial integrity. MCC physically interacts with the E-cadherin/beta-catenin complex (established by co-immunoprecipitation). Loss of MCC enhances hepatocyte growth factor-induced cell scatter and tumor cell invasiveness, which is abrogated by the Src/Abl inhibitor dasatinib.\",\n      \"method\": \"siRNA knockdown, co-immunoprecipitation, dispase assay, transepithelial electrical resistance, organotypic invasion assay, pharmacological rescue\",\n      \"journal\": \"Oncogene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP establishing direct protein complex, loss-of-function with multiple defined phenotypic readouts, single lab\",\n      \"pmids\": [\"29035389\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Crystal structures of the Scribble PDZ1 domain bound to the unphosphorylated MCC PDZ-binding motif (PBM) and to phosphorylated MCC (phospho-Ser at -1 position) were determined. Scribble PDZ1 and PDZ3 are the major domains interacting with the MCC PBM. Phosphorylation at the -1 Ser position of MCC has only a minor effect on binding affinity to Scribble PDZ domains; the phospho-Ser makes no major contacts with PDZ1 in the structure, suggesting phosphorylation's functional impact extends beyond simple affinity modulation.\",\n      \"method\": \"Crystal structure determination, affinity measurements (ITC or equivalent), systematic binding assays across all four Scribble PDZ domains\",\n      \"journal\": \"The FEBS journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structures with functional validation by affinity measurements, multiple orthogonal methods, directly testing phosphorylation impact\",\n      \"pmids\": [\"31317644\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"A novel MCC paralogue, MCC2, was identified by yeast two-hybrid screening as a binding partner of the PDZ-domain protein AIE-75. MCC2 binds the first PDZ domain of AIE-75 via its C-terminal residues (-DTFL). In contrast, MCC1 (canonical MCC) does not bind AIE-75, indicating distinct interaction profiles for the two paralogues.\",\n      \"method\": \"Yeast two-hybrid screening, interaction domain mapping\",\n      \"journal\": \"Gene\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single yeast two-hybrid method, no in vivo confirmation reported, single lab\",\n      \"pmids\": [\"11311560\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"MCC (Mutated in Colorectal Cancer) encodes a cytoplasmic PDZ domain-containing phosphoprotein that negatively regulates cell cycle progression from G1 to S phase, interacts with the E-cadherin/β-catenin complex to maintain cell-cell adhesion, sequesters the β-catenin coactivator DBC1 in the cytoplasm to suppress β-catenin transcriptional activity via SIRT1-mediated deacetylation, and functions as an intracellular effector of non-canonical Wnt5b/Vangl2/Ror2 signaling (upstream of RhoA/JNK) during embryonic convergence and extension; its PDZ-binding motif mediates phosphorylation-regulated interactions with Scrib and Myosin-IIB to control lamellipodia formation and cell migration.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MCC (Mutated in Colorectal Cancer) is a cytoplasmic PDZ-binding-motif phosphoprotein that integrates cell-cycle control, cell-cell adhesion, and non-canonical Wnt signaling at epithelial membranes [#0, #5, #6]. It was first defined as a 100-kDa phosphoprotein whose phosphorylation rises during the G1-to-S transition, and whose wild-type form blocks serum-induced G1-to-S progression while a colorectal-tumor-derived mutant fails to do so [#0]. MCC localizes to apical microvilli and lateral cell borders in epithelia and concentrates at the active migratory edge of cells [#1, #3]. Through its C-terminal PDZ-binding motif it engages the Scribble polarity protein, and Ser828 phosphorylation at the -1 position regulates a MCC-Scribble-Myosin-IIB complex that governs lamellipodia formation and directed migration [#2, #3]; crystallography of Scribble PDZ1 bound to phosphorylated and unphosphorylated MCC shows the phospho-Ser makes no major PDZ contacts, indicating that phosphorylation acts beyond simple affinity tuning [#7]. MCC restrains Wnt/\\u03b2-catenin output by two routes: it physically associates with and stabilizes the E-cadherin/\\u03b2-catenin adhesion complex to maintain epithelial integrity and limit HGF-induced scatter and invasion [#6], and it sequesters the \\u03b2-catenin coactivator DBC1 in the cytoplasm, reducing \\u03b2-catenin K49 acetylation via SIRT1 to suppress its transcriptional activity [#4]. In zebrafish gastrulation MCC binds the Vangl2 cytoplasmic tail and acts as an intracellular effector of Wnt5b/Vangl2/Ror2 planar cell polarity signaling upstream of RhoA/JNK during convergence and extension [#5]. Disease-associated MCC mutations impair both its G1-to-S block and its DBC1/\\u03b2-catenin repressor function [#0, #4].\",\n  \"teleology\": [\n    {\n      \"year\": 1996,\n      \"claim\": \"Established that MCC is a cell-cycle-regulated phosphoprotein that actively restrains the G1-to-S transition, and that a tumor-derived mutation abolishes this control.\",\n      \"evidence\": \"Phosphorylation analysis across synchronized cell cycle plus wild-type versus mutant overexpression in NIH3T3 cells\",\n      \"pmids\": [\"8626604\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"The kinase phosphorylating MCC and the molecular target of its G1-S block were not identified\", \"Endogenous loss-of-function consequence not tested\"]\n    },\n    {\n      \"year\": 1999,\n      \"claim\": \"Defined MCC's subcellular and tissue distribution, placing it at apical/lateral epithelial membranes and linking it to differentiation beyond cell-cycle control.\",\n      \"evidence\": \"Immunohistochemistry and immunoelectron microscopy across mouse epithelia and neuronal cells, plus NGF-induced PC12 differentiation\",\n      \"pmids\": [\"10449536\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Membrane-targeting mechanism unknown\", \"Functional role in differentiation inferred from expression, not perturbation\"]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"Identified Scribble as a PDZ-dependent MCC partner and tied MCC to directed epithelial migration, distinguishing its pathway from canonical Rac1/Cdc42/PAK signaling.\",\n      \"evidence\": \"Yeast two-hybrid, co-IP, colocalization, and siRNA migration assays in T47D cells\",\n      \"pmids\": [\"19555689\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Downstream effectors of the MCC-Scrib axis in migration not defined\", \"Single cell-line context\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Mapped Ser828 in the MCC PDZ-binding motif as a phosphorylation switch controlling a MCC-Scrib-Myosin-IIB complex governing lamellipodia formation.\",\n      \"evidence\": \"Phospho-site mapping, phosphomimetic/phosphodeficient mutagenesis, co-IP, fractionation, and lamellipodia assays\",\n      \"pmids\": [\"22480440\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Kinase responsible for Ser828 phosphorylation not identified\", \"Mechanistic link between PBM phosphorylation and Myosin-IIB cortical accumulation not resolved\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Revealed a mechanism by which MCC suppresses \\u03b2-catenin transcriptional output: cytoplasmic sequestration of DBC1 leading to SIRT1-dependent \\u03b2-catenin deacetylation.\",\n      \"evidence\": \"Co-IP, RNAi, fractionation, reporter and acetylation assays, and pharmacological SIRT1 inhibition\",\n      \"pmids\": [\"24824780\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether MCC directly regulates SIRT1 or acts only through DBC1 relocalization not resolved\", \"Single-lab biochemistry\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Placed MCC as an intracellular effector of non-canonical Wnt/PCP signaling by demonstrating direct Vangl2 binding and epistasis upstream of RhoA/JNK during convergence and extension.\",\n      \"evidence\": \"Zebrafish morpholino knockdown, reciprocal overexpression rescue, Mcc-Vangl2 co-IP, and RhoA/JNK epistasis\",\n      \"pmids\": [\"25183869\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How Mcc transduces Vangl2 engagement to RhoA/JNK activation not defined\", \"Morpholino-based knockdown without genetic mutant confirmation\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Showed MCC physically stabilizes the E-cadherin/\\u03b2-catenin adhesion complex and that its loss licenses HGF-driven, Src/Abl-dependent invasion.\",\n      \"evidence\": \"siRNA knockdown, co-IP, dispase and TEER adhesion assays, organotypic invasion, and dasatinib rescue in HCT116 cells\",\n      \"pmids\": [\"29035389\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct versus indirect nature of the MCC-cadherin association not dissected\", \"Mechanism by which MCC loss activates Src/Abl signaling unknown\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Provided structural detail of the MCC-Scribble interface, showing that PBM Ser828 phosphorylation only weakly affects binding affinity, implying a regulatory function beyond simple affinity modulation.\",\n      \"evidence\": \"Crystal structures of Scribble PDZ1 with phospho- and unphospho-MCC PBM plus affinity measurements across all four Scribble PDZ domains\",\n      \"pmids\": [\"31317644\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The non-affinity mechanism by which phosphorylation alters MCC function in cells not established\", \"Structural basis of MCC-Myosin-IIB coupling not addressed\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The kinase(s) controlling MCC's cell-cycle and PBM phosphorylation, and how its adhesion, \\u03b2-catenin-repressive, and PCP functions are coordinated in a single cell, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No upstream kinase identified for any MCC phosphosite\", \"No unified model linking G1-S control, adhesion, DBC1 sequestration, and Wnt/PCP\", \"MCC2 paralogue function in vivo uncharacterized\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [2, 3, 5]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [4, 6]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [1, 2, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [4, 5, 6]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-1500931\", \"supporting_discovery_ids\": [6]}\n    ],\n    \"complexes\": [\n      \"MCC-Scribble-Myosin-IIB complex\",\n      \"E-cadherin/\\u03b2-catenin complex\"\n    ],\n    \"partners\": [\n      \"SCRIB\",\n      \"MYH10\",\n      \"CCAR2\",\n      \"VANGL2\",\n      \"CDH1\",\n      \"CTNNB1\",\n      \"NHERF1\",\n      \"EZR\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":7,"faith_total":7,"faith_pct":100.0}}