ArticleCommunications biology2022
CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- Transport mechanism of the SLC4 proteins-Lessons from recent structural and computational studies.The Journal of biological chemistry · 2026Review
- Efficient sampling of large-scale transition pathways and intermediate conformations in sub-mesoscopic protein complexes.Nature communications · 2026Article
- N-Glycosylation of Band 3 is essential for the binding of Ganoderma lucidum immunomodulatory protein rLZ-8.Applied microbiology and biotechnology · 2026Article
- Impact of anionic lipids on the energy landscape of conformational transition in anion exchanger 1 (AE1).Nature communications · 2025Article
- CryoEM and computational modeling structural insights into the pH regulator NBCn1.Nature communications · 2025Article
- Molecular determinants of [Formula: see text] and cation transport in the human cation-dependent ClAmerican journal of physiology. Cell physiology · 2025Article
- Role of channels in the ObioRxiv : the preprint server for biology · 2025Article
- Urinary sodium wasting and disrupted collecting duct function in mice with distal renal tubular acidosis mutations.Disease models & mechanisms · 2025Article
- The Bor1 elevator transport cycle is subject to autoinhibition and activation.Nature communications · 2024Article
- Cryo-EM structures of the human band 3 transporter indicate a transport mechanism involving the coupled movement of chloride and bicarbonate ions.PLoS biology · 2024Article
- The structural insight into the functional modulation of human anion exchanger 3.Nature communications · 2024Article
- Molecular dynamics simulations of lipid-protein interactions in SLC4 proteins.Biophysical journal · 2024Article
- Structural and functional insights into the lipid regulation of human anion exchanger 2.Nature communications · 2024Article
- Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1.Nature plants · 2024Article
- On the substrate turnover rate of NBCe1 and AE1 SLC4 transporters: structure-function considerations.Frontiers in physiology · 2024Article
- Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIPNature communications · 2023Article
- The structural basis of the pH-homeostasis mediated by the ClNature communications · 2023Article
- Novel Variant of theBiomedicines · 2023Article
- Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties.Membranes · 2023Article
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Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
Abstract
Anion exchanger 1 (AE1, band 3) is a major membrane protein of red blood cells and plays a key role in acid-base homeostasis, urine acidification, red blood cell shape regulation, and removal of carbon dioxide during respiration. Though structures of the transmembrane domain (TMD) of three SLC4 transporters, including AE1, have been resolved previously in their outward-facing (OF) state, no mammalian SLC4 structure has been reported in the inward-facing (IF) conformation. Here we present the cryoEM structures of full-length bovine AE1 with its TMD captured in both IF and OF conformations. Remarkably, both IF-IF homodimers and IF-OF heterodimers were detected. The IF structures feature downward movement in the core domain with significant unexpected elongation of TM11. Molecular modeling and structure guided mutagenesis confirmed the functional significance of residues involved in TM11 elongation. Our data provide direct evidence for an elevator-like mechanism of ion transport by an SLC4 family member.
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