PT  - JOURNAL ARTICLE
AU  - Vallese, F.
AU  - Kim, K.
AU  - Yen, L.Y.
AU  - Johnston, J.D.
AU  - Noble, A.J.
AU  - Calì, T.
AU  - Clarke, O.B.
TI  - Architecture of the human erythrocyte ankyrin-1 complex
AID  - 10.1101/2022.02.10.479914
DP  - 2022 Jan 01
TA  - bioRxiv
PG  - 2022.02.10.479914
4099  - http://biorxiv.org/content/early/2022/02/10/2022.02.10.479914.short
4100  - http://biorxiv.org/content/early/2022/02/10/2022.02.10.479914.full
AB  - 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 StatementThe authors have declared no competing interest.