ArticleBioscience reports2015
Identification of residues in ABCG2 affecting protein trafficking and drug transport, using co-evolutionary analysis of ABCG sequences.
Article in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed.
- ABCG2 transporter: Structural and functional associations with gout (Review).International journal of molecular medicine · 2026Review
- Development of a High-Sensitivity Electrochemical Biosensor for Domoic Acid and Its Cellular Impact on Human Stem and Neuron-Like Cells.Food science & nutrition · 2026Article
- Hydroxygenkwanin Improves the Efficacy of Cytotoxic Drugs in ABCG2-Overexpressing Multidrug-Resistant Cancer Cells.International journal of molecular sciences · 2022Article
- Analysis of Sequence Divergence in Mammalian ABCGs Predicts a Structural Network of Residues That Underlies Functional Divergence.International journal of molecular sciences · 2021Article
- A NovelLife (Basel, Switzerland) · 2021Review
- The first intracellular loop is essential for the catalytic cycle of the human ABCG2 multidrug resistance transporter.FEBS letters · 2020Article
- Review
- Application of fluorescence correlation spectroscopy to study substrate binding in styrene maleic acid lipid copolymer encapsulated ABCG2.Biochimica et biophysica acta. Biomembranes · 2020Article
- ABCG2 transports anticancer drugs via a closed-to-open switch.Nature communications · 2020Article
- ABCG2 requires a single aromatic amino acid to "clamp" substrates and inhibitors into the binding pocket.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Disruption of the Unique ABCG-Family NBD:NBD Interface Impacts Both Drug Transport and ATP Hydrolysis.International journal of molecular sciences · 2020Article
- The ABCG2 multidrug transporter is a pump gated by a valve and an extracellular lid.Nature communications · 2019Article
- Article
- Residues contributing to drug transport by ABCG2 are localised to multiple drug-binding pockets.The Biochemical journal · 2018Article
- Structural basis of small-molecule inhibition of human multidrug transporter ABCG2.Nature structural & molecular biology · 2018Article
- Structure-function relationships in ABCG2: insights from molecular dynamics simulations and molecular docking studies.Scientific reports · 2017Article
- The structure of the human ABC transporter ABCG2 reveals a novel mechanism for drug extrusion.Scientific reports · 2017Article
- 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
- The multidrug transporter ABCG2: still more questions than answers.Biochemical Society transactions · 2016Review
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ABCG2 is an ABC (ATP-binding cassette) transporter with a physiological role in urate transport in the kidney and is also implicated in multi-drug efflux from a number of organs in the body. The trafficking of the protein and the mechanism by which it recognizes and transports diverse drugs are important areas of research. In the current study, we have made a series of single amino acid mutations in ABCG2 on the basis of sequence analysis. Mutant isoforms were characterized for cell surface expression and function. One mutant (I573A) showed disrupted glycosylation and reduced trafficking kinetics. In contrast with many ABC transporter folding mutations which appear to be 'rescued' by chemical chaperones or low temperature incubation, the I573A mutation was not enriched at the cell surface by either treatment, with the majority of the protein being retained in the endoplasmic reticulum (ER). Two other mutations (P485A and M549A) showed distinct effects on transport of ABCG2 substrates reinforcing the role of TM helix 3 in drug recognition and transport and indicating the presence of intracellular coupling regions in ABCG2.
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