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. Epub 2008 Mar 17.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blood Proteins / genetics
  • Blood Proteins / metabolism*
  • Calmodulin-Binding Proteins / metabolism*
  • Cell Line
  • Cytoskeleton / metabolism*
  • Erythrocyte Membrane / metabolism*
  • Glucose Transporter Type 1 / genetics
  • Glucose Transporter Type 1 / metabolism*
  • Humans
  • Mice
  • Protein Binding
  • Proteomics

Substances

  • Blood Proteins
  • Calmodulin-Binding Proteins
  • Glucose Transporter Type 1
  • adducin