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 Blood, 27 August 2009, Vol. 114, No. 9, pp. 1904-1912.
Prepublished online as a Blood First Edition Paper on June 30, 2009; DOI 10.1182/blood-2009-02-203216.

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RED CELLS, IRON, AND ERYTHROPOIESIS

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

William A. Anong1,*, Taina Franco1,*, Haiyan Chu1,*, Tahlia L. Weis1, Emily E. Devlin2, David M. Bodine2, Xiuli An3, Narla Mohandas3, and Philip S. Low1

1 Department of Chemistry, Purdue University, West Lafayette, IN; 2 Genetics and Molecular Biology Branch, National Human Genome Research Institute, National Institutes of Health, Bethesda MD; and 3 Laboratory of Physiology, New York Blood Center, NY

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 spontaneous membrane fragmentation, 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.


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