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Architecture of the human erythrocyte ankyrin-1 complex

F. Vallese, View ORCID ProfileK. Kim, L.Y. Yen, J.D. Johnston, View ORCID ProfileA.J. Noble, T. Calì, View ORCID ProfileO.B. Clarke
doi: https://doi.org/10.1101/2022.02.10.479914
F. Vallese
1Department of Anesthesiology, Columbia University Irving Medical Center; New York, NY,10032, USA
2Department of Physiology and Cellular Biophysics, Columbia University; New York, NY, 10032, USA
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K. Kim
2Department of Physiology and Cellular Biophysics, Columbia University; New York, NY, 10032, USA
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L.Y. Yen
2Department of Physiology and Cellular Biophysics, Columbia University; New York, NY, 10032, USA
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J.D. Johnston
2Department of Physiology and Cellular Biophysics, Columbia University; New York, NY, 10032, USA
3Simons Electron Microscopy Center, New York Structural Biology Center; New York, NY, USA
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A.J. Noble
3Simons Electron Microscopy Center, New York Structural Biology Center; New York, NY, USA
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  • ORCID record for A.J. Noble
T. Calì
4Department of Biomedical Sciences, University of Padua; 35131 Padua, Italy
5Padua Neuroscience Center (PNC), University of Padua; 35131 Padua, Italy
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O.B. Clarke
1Department of Anesthesiology, Columbia University Irving Medical Center; New York, NY,10032, USA
2Department of Physiology and Cellular Biophysics, Columbia University; New York, NY, 10032, USA
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  • For correspondence: olibclarke@gmail.com
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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 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.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
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Posted February 10, 2022.
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Architecture of the human erythrocyte ankyrin-1 complex
F. Vallese, K. Kim, L.Y. Yen, J.D. Johnston, A.J. Noble, T. Calì, O.B. Clarke
bioRxiv 2022.02.10.479914; doi: https://doi.org/10.1101/2022.02.10.479914
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Architecture of the human erythrocyte ankyrin-1 complex
F. Vallese, K. Kim, L.Y. Yen, J.D. Johnston, A.J. Noble, T. Calì, O.B. Clarke
bioRxiv 2022.02.10.479914; doi: https://doi.org/10.1101/2022.02.10.479914

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