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  2. Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1

Dematin and adducin provide a novel link between the spectrin cytoskeleton and human erythrocyte membrane by directly interacting with glucose transporter-1

  • J Biol Chem. 2008 May 23;283(21):14600-9. doi: 10.1074/jbc.M707818200.
Anwar A Khan 1 Toshihiko Hanada Morvarid Mohseni Jong-Jin Jeong Lixiao Zeng Massimiliano Gaetani Donghai Li Brent C Reed David W Speicher Athar H Chishti
Affiliations

Affiliation

  • 1 Department of Pharmacology, University of Illinois Cancer Center, University of Illinois College of Medicine, Chicago, IL 60612, USA.
Abstract

Dematin and adducin are actin-binding proteins located at the spectrin-actin junctions, also called the junctional complex, in the erythrocyte membrane. Here we propose a new model whereby dematin and adducin link the junctional complex to human erythrocyte plasma membrane. Using a combination of surface labeling, immunoprecipitation, and vesicle proteomics approaches, we have identified glucose transporter-1 as the receptor for dematin and adducin in the human erythrocyte membrane. This finding is the first description of a transmembrane protein that binds to dematin and adducin, thus providing a rationale for the attachment of the junctional complex to the lipid bilayer. Because homologues of dematin, adducin, and glucose transporter-1 exist in many non-erythroid cells, we propose that a conserved mechanism may exist that couples sugar and other related transporters to the actin Cytoskeleton.

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