{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Ma WH"],"funding":["National Natural Science Foundation of China","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["72-93"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12765898"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["36(1)"],"pubmed_abstract":["Colorectal cancer (CRC) remains largely refractory to immune-checkpoint blockade, with adenomatous polyposis coli (APC) mutations present in 80%-90% of cases. Loss of APC was previously thought to promote tumor progression mainly through deregulated Wnt/β-catenin signaling. Here, we report that APC loss leads to inhibition of CD8<sup>+</sup> T cell infiltration and CRC immune evasion through the dephosphorylation of signal transducers and activators of transcription 1 (STAT1) by protein tyrosine phosphatase non-receptor type 13 (PTPN13), independently of β-catenin. Peptides containing the last 11 C-terminal amino acid (aa) residues of APC (APC11) bind directly to PTPN13 to block PTPN13-STAT1 interactions and facilitate STAT1 phosphorylation, interferon regulatory factor-1 (IRF1) expression"],"journal":["Cell research"],"pubmed_title":["Targeting PTPN13 with 11-amino-acid peptides of C-terminal APC prevents immune evasion of colorectal cancer."],"pmcid":["PMC12765898"],"funding_grant_id":["82441036"],"pubmed_authors":["Li G","Jing L","Zhou WJ","Liu HJ","Shen RF","Luo TY","Wu D","Li K","Sun X","Wu ZK","Bai X","Qiu X","Ma WH","He Y","Mou T","Xu ZL","Gao Y","Li WY","Chen YH","Wang LJ","Wang W","Chen T"],"additional_accession":[]},"is_claimable":false,"name":"Targeting PTPN13 with 11-amino-acid peptides of C-terminal APC prevents immune evasion of colorectal cancer.","description":"Colorectal cancer (CRC) remains largely refractory to immune-checkpoint blockade, with adenomatous polyposis coli (APC) mutations present in 80%-90% of cases. Loss of APC was previously thought to promote tumor progression mainly through deregulated Wnt/β-catenin signaling. Here, we report that APC loss leads to inhibition of CD8<sup>+</sup> T cell infiltration and CRC immune evasion through the dephosphorylation of signal transducers and activators of transcription 1 (STAT1) by protein tyrosine phosphatase non-receptor type 13 (PTPN13), independently of β-catenin. Peptides containing the last 11 C-terminal amino acid (aa) residues of APC (APC11) bind directly to PTPN13 to block PTPN13-STAT1 interactions and facilitate STAT1 phosphorylation, interferon regulatory factor-1 (IRF1) expression","dates":{"release":"2026-01-01T00:00:00Z","publication":"2026 Jan","modification":"2026-06-06T20:03:15.346Z","creation":"2026-06-04T03:14:49.679Z"},"accession":"S-EPMC12765898","cross_references":{"pubmed":["41486293"],"doi":["10.1038/s41422-025-01206-4"]}}