{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Padi SKR"],"funding":["NINDS NIH HHS","NIH HHS","NIGMS NIH HHS"],"pagination":["1373-1382"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12350174"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(8)"],"pubmed_abstract":["Phosphoprotein phosphatases (PPPs) achieve specificity by binding substrates and regulators using PPP-specific short motifs. Protein phosphatase 2A (PP2A) is a highly conserved phosphatase that regulates cell signaling and is a tumor suppressor. Here, we use cryo-electron microscopy and nuclear magnetic resonance (NMR) spectroscopy to investigate the mechanisms of human p107 substrate and Eya3 regulator recruitment to the PP2A:B55 holoenzyme. We show that, while they associate with B55 using a common set of interaction pockets, the mechanism of substrate and regulator binding differs and is distinct from that observed for PP2A:B56 and other PPPs. We also identify the core B55 recruitment motif in Eya3 proteins, a sequence conserved amongst the Eya family. Lastly, using NMR-based dephosphor"],"journal":["Nature structural & molecular biology"],"pubmed_title":["Cryo-EM structures of PP2A:B55 with p107 and Eya3 define substrate recruitment."],"pmcid":["PMC12350174"],"funding_grant_id":["R24 GM154192","S10 OD032156","U24 GM129539","R01 NS124666","R01 GM144483","R01 GM144379","R24 GM154185"],"pubmed_authors":["Padi SKR","Peti W","Godek RJ","Page R"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structures of PP2A:B55 with p107 and Eya3 define substrate recruitment.","description":"Phosphoprotein phosphatases (PPPs) achieve specificity by binding substrates and regulators using PPP-specific short motifs. Protein phosphatase 2A (PP2A) is a highly conserved phosphatase that regulates cell signaling and is a tumor suppressor. Here, we use cryo-electron microscopy and nuclear magnetic resonance (NMR) spectroscopy to investigate the mechanisms of human p107 substrate and Eya3 regulator recruitment to the PP2A:B55 holoenzyme. We show that, while they associate with B55 using a common set of interaction pockets, the mechanism of substrate and regulator binding differs and is distinct from that observed for PP2A:B56 and other PPPs. We also identify the core B55 recruitment motif in Eya3 proteins, a sequence conserved amongst the Eya family. Lastly, using NMR-based dephosphor","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-07-15T10:49:39.526Z","creation":"2026-07-04T03:11:57.229Z"},"accession":"S-EPMC12350174","cross_references":{"pubmed":["40247147"],"doi":["10.1038/s41594-025-01535-3"]}}