ArticleiScience2025
The human ABCG2 transporter engages three gates to control multidrug extrusion.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Cryo-EM structures of Cdr1 reveal snapshots of substrate transport and diverse inhibitor recognition.Science advances · 2026Article
- In-Silico and Functional Characterization of EcdLp, an ABC Transporter of Aspergillus nidulans NRRL11440.Current microbiology · 2026Article
- ABCG2 Transporter: From Structure to Function-Current Insights and Open Questions.International journal of molecular sciences · 2025Review
- Revisiting the Role of the Leucine Plug/Valve in the Human ABCG2 Multidrug Transporter.International journal of molecular sciences · 2025Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human ABCG2 transporter plays roles in physiological detoxification across barriers and in anticancer multidrug resistance. The translocation pathway for drug extrusion and its gating mechanism remains elusive. Here, we demonstrate that the ABCG2 multidrug transporter holds two cavities that are delineated by three regulatory gates, indicating a substrate translocation channel. Drugs are trapped in the central cavity after entering through the pivotal intracellular entry gate. This flexible cavity is surrounded by a cluster of three highly conserved phenylalanines. Their aromatic side chains enact a "clamp-push-seal" motion to ensure unidirectional substrate movement. The unique residues T435 and N436 act as critical selectors for ligands, determining the broad substrate specificity. The upper cavity is covered by the lid architecture, constituting the final gate before multidrug extrusion. This work unravels deep mechanistic details on how the translocation channel utilizes pivotal gating steps, including the sequence of events that drive ABCG2-mediated multidrug efflux.
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Registered trials
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