RT Journal Article
SR Electronic
T1 Architecture of the human erythrocyte ankyrin-1 complex
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2022.02.10.479914
DO 10.1101/2022.02.10.479914
A1 Vallese, F.
A1 Kim, K.
A1 Yen, L.Y.
A1 Johnston, J.D.
A1 Noble, A.J.
A1 Calì, T.
A1 Clarke, O.B.
YR 2022
UL http://biorxiv.org/content/early/2022/02/10/2022.02.10.479914.abstract
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.