Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion

William A. Anong, Taina Franco, Haiyan Chu, Tahlia L. Weis, Emily E. Devlin, David M. Bodine, Xiuli An, Narla Mohandas, Philip S. Low

Research output: Contribution to journalArticle

105 Scopus citations

Abstract

The erythrocyte membrane skeleton is the best understood cytoskeleton. Because its protein components have homologs in virtually all other cells, the membrane serves as a fundamental model of biologic membranes. Modern textbooks portray the membrane as a 2-dimensional spectrin-based membrane skeleton attached to a lipid bilayer through 2 linkages: band 3-ankyrin-β-spectrin and glycophorin C-protein 4.1-β-spectrin.1-7 Although evidence supports an essential role for the first bridge in regulating membrane cohesion, rupture of the glycophorin C-protein 4.1 interaction has little effect on membrane stability.8 We demonstrate the existence of a novel band 3-adducin-spectrin bridge that connects the spectrin/actin/protein 4.1 junctional complex to the bilayer. As rupture of this bridge leads to spontaneousmembranefragmentation, we conclude that the band 3-adducin-spectrin bridge is important to membrane stability. The required relocation of part of the band 3 population to the spectrin/actin junctional complex and its formation of a new bridge with adducin necessitates a significant revision of accepted models of the erythrocyte membrane.

Original languageEnglish (US)
Pages (from-to)1904-1912
Number of pages9
JournalBlood
Volume114
Issue number9
DOIs
StatePublished - 2009

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

Fingerprint Dive into the research topics of 'Adducin forms a bridge between the erythrocyte membrane and its cytoskeleton and regulates membrane cohesion'. Together they form a unique fingerprint.

Cite this