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Architecture of the human erythrocyte ankyrin-1 complex.
Vallese, Francesca; Kim, Kookjoo; Yen, Laura Y; Johnston, Jake D; Noble, Alex J; Calì, Tito; Clarke, Oliver Biggs.
Afiliación
  • Vallese F; Department of Anesthesiology, Columbia University Irving Medical Center, New York, NY, USA.
  • Kim K; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, USA.
  • Yen LY; Irving Institute for Clinical and Translational Research, Columbia University, New York, NY, USA.
  • Johnston JD; Department of Anesthesiology, Columbia University Irving Medical Center, New York, NY, USA.
  • Noble AJ; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, USA.
  • Calì T; Irving Institute for Clinical and Translational Research, Columbia University, New York, NY, USA.
  • Clarke OB; Department of Physiology and Cellular Biophysics, Columbia University, New York, NY, USA.
Nat Struct Mol Biol ; 29(7): 706-718, 2022 07.
Article en En | MEDLINE | ID: mdl-35835865
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína 1 de Intercambio de Anión de Eritrocito / Ancirinas Límite: Humans Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteína 1 de Intercambio de Anión de Eritrocito / Ancirinas Límite: Humans Idioma: En Revista: Nat Struct Mol Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos