{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tambe V"],"funding":["NCI NIH HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["100007"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11934288"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["107(2)"],"pubmed_abstract":["Organic anion transporting polypeptide (OATP) 1B1 is crucial for hepatic uptake of many drugs and endogenous substrates. The clinically relevant OATP1B1 c.521 T>C (V174A) polymorphism exhibits reduced transport activity in vitro and in vivo in humans. Previously, we reported increased total phosphorylation of V174A-OATP1B1 compared to wild-type (WT)-OATP1B1, although the differentially phosphorylated sites remain to be identified. Lysine-acetylation, a key posttranslational modification (PTM), has not been investigated in OATP1B1. This study aimed to identify differential PTMs of WT-OATP1B1 and V174A-OATP1B1 by quantitatively comparing the relative abundance of modified peptides using liquid chromatography-tandem mass spectrometry-based proteomics and to assess the impact of these PTMs on "],"journal":["Molecular pharmacology"],"pubmed_title":["Regulation of organic anion transporting polypeptide 1B1 transport function by concurrent phosphorylation and lysine-acetylation: A novel posttranslational regulation mechanism."],"pmcid":["PMC11934288"],"funding_grant_id":["R01 GM094268","R01 GM146956","S10 OD024999","P30 CA225520"],"pubmed_authors":["Tambe V","Xu C","Soderblom EJ","Yue W","Kayesh R","Aditya V"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of organic anion transporting polypeptide 1B1 transport function by concurrent phosphorylation and lysine-acetylation: A novel posttranslational regulation mechanism.","description":"Organic anion transporting polypeptide (OATP) 1B1 is crucial for hepatic uptake of many drugs and endogenous substrates. The clinically relevant OATP1B1 c.521 T>C (V174A) polymorphism exhibits reduced transport activity in vitro and in vivo in humans. Previously, we reported increased total phosphorylation of V174A-OATP1B1 compared to wild-type (WT)-OATP1B1, although the differentially phosphorylated sites remain to be identified. Lysine-acetylation, a key posttranslational modification (PTM), has not been investigated in OATP1B1. This study aimed to identify differential PTMs of WT-OATP1B1 and V174A-OATP1B1 by quantitatively comparing the relative abundance of modified peptides using liquid chromatography-tandem mass spectrometry-based proteomics and to assess the impact of these PTMs on ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2025-07-11T03:04:03.066Z","creation":"2025-07-11T03:04:03.066Z"},"accession":"S-EPMC11934288","cross_references":{"pubmed":["40023514"],"doi":["10.1016/j.molpha.2024.100007"]}}