Architecture of the human erythrocyte ankyrin-1 complex

The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures...

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Bibliographic Details
Published inbioRxiv
Main Authors Vallese, Francesca, Kim, Kookjoo, Yen, Laura Y, Johnston, Jake D, Noble, Alex J, Cali, Tito, Clarke, Oliver B
Format Paper
LanguageEnglish
Published Cold Spring Harbor Cold Spring Harbor Laboratory Press 10.02.2022
Subjects
Actin
Ankyrins
Cytoskeleton
Erythrocytes
Glycoproteins
Lipid bilayers
Membrane proteins
Spectrin
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Summary:The stability and shape of the erythrocyte membrane is provided by the ankyrin-1 complex, but how it tethers the spectrin-actin cytoskeleton to the lipid bilayer and the nature of its association with the band 3 anion exchanger and the Rhesus glycoproteins remains unknown. Here we present structures of ankyrin-1 complexes purified from human erythrocytes. We reveal the architecture of a core complex of ankyrin-1, the Rhesus proteins RhAG and RhCE, the band 3 anion exchanger, protein 4.2 and glycophorin A. The distinct T-shaped conformation of membrane-bound ankyrin-1 facilitates recognition of RhCE and unexpectedly, the water channel aquaporin-1. Together, our results uncover the molecular details of ankyrin-1 association with the erythrocyte membrane, and illustrate the mechanism of ankyrin-mediated membrane protein clustering. Competing Interest Statement The authors have declared no competing interest.
DOI:10.1101/2022.02.10.479914