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

作者：Anong William A; Franco Taina; Chu Haiyan; Weis Tahlia L; Devlin Emily E; Bodine David M; An Xiuli; Mohandas Narla; Low Philip S^*

来源：Blood, 2009, 114(9): 1904-1912.

DOI：10.1182/blood-2009-02-203216

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-beta-spectrin and glycophorin C-protein 4.1-beta-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. (Blood. 2009; 114: 1904-1912)

• 出版日期2009-8-27