ArticlePloS one2012
N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The trial behind it
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Who cites it
26 citing papers in PubMed, 65 citations in OpenAlex.
- Loss of palmitoylation impacts the interaction between the organic anion transporting polypeptide (OATP) 1B1 and OATP1B3.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Altered Bile Acid Transport in Liver Disease.Biomedicines · 2026Review
- Review
- Phosphorylation dynamics of sodium-independent organic anion transporter SLCO4A1 and its role in diseases: a review.Frontiers in systems biology · 2026Review
- Organic anion transporting polypeptides: Pharmacology, toxicology, structure, and transport mechanisms.Pharmacological reviews · 2025Review
- Importance of N-Glycosylation for the Expression and Function of Human Organic Anion Transporting Polypeptide 2B1.ACS pharmacology & translational science · 2023Article
- Comparative Modelling of Organic Anion Transporting Polypeptides: Structural Insights and Comparison of Binding Modes.Molecules (Basel, Switzerland) · 2022Article
- Innovative approaches and recent advances in the study of ontogeny of drug metabolism and transport.British journal of clinical pharmacology · 2022Review
- Regulation of Drug Transport Proteins-From Mechanisms to Clinical Impact: A White Paper on Behalf of the International Transporter Consortium.Clinical pharmacology and therapeutics · 2022Review
- Pharmacoproteomics of Brain Barrier Transporters and Substrate Design for the Brain Targeted Drug Delivery.Pharmaceutical research · 2022Review
- Is It Time to Use Modeling of Cellular Transporter Homeostasis to Inform Drug-Drug Interaction Studies: Theoretical Considerations.The AAPS journal · 2021Article
- Post-translational regulation of the major drug transporters in the families of organic anion transporters and organic anion-transporting polypeptides.The Journal of biological chemistry · 2020Review
- Alternative Splicing of the SLCO1B1 Gene: An Exploratory Analysis of Isoform Diversity in Pediatric Liver.Clinical and translational science · 2020Article
- Characterization of tick organic anion transporting polypeptides (OATPs) upon bacterial and viral infections.Parasites & vectors · 2018Article
- Regulation of Organic Anion Transporting Polypeptides (OATP) 1B1- and OATP1B3-Mediated Transport: An Updated Review in the Context of OATP-Mediated Drug-Drug Interactions.International journal of molecular sciences · 2018Review
- Trafficking and other regulatory mechanisms for organic anion transporting polypeptides and organic anion transporters that modulate cellular drug and xenobiotic influx and that are dysregulated in disease.British journal of pharmacology · 2017Review
- Impaired N-linked glycosylation of uptake and efflux transporters in human non-alcoholic fatty liver disease.Liver international : official journal of the International Association for the Study of the Liver · 2017Article
- Loops and layers of post-translational modifications of drug transporters.Advanced drug delivery reviews · 2017Review
- Role of OATP transporters in steroid uptake by prostate cancer cells in vivo.Prostate cancer and prostatic diseases · 2017Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins. Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins. However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins. In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver. Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process. Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity. Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.