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Architecture of the human erythrocyte ankyrin-1 complex.

ABSTRACT: 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, glycophorin A and glycophorin B. 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.

SUBMITTER: Vallese F

PROVIDER: S-EPMC10373098 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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Architecture of the human erythrocyte ankyrin-1 complex.

Vallese Francesca F Kim Kookjoo K Yen Laura Y LY Johnston Jake D JD Noble Alex J AJ Calì Tito T Clarke Oliver Biggs OB

Nature structural & molecular biology 20220714 7

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, glycoph ...[more]

PMID: 35835865

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Architecture of the human erythrocyte ankyrin-1 complex

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