Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide

@article{Anderson1985RegulationOT,
  title={Regulation of the association of membrane skeletal protein 4.1 with glycophorin by a polyphosphoinositide},
  author={Richard A. Anderson and Vincent T. Marchesi},
  journal={Nature},
  year={1985},
  volume={318},
  pages={295-298}
}
Many of the physical properties of the erythrocyte membrane appear to depend on the membrane skeleton, which is attached to the membrane through associations with transmembrane proteins1–5. A membrane skeletal protein, protein 4.1, is pivotal in the assembly of the membrane skeleton because of its ability to promote associations between spectrin and actin5–9. Protein 4.1 also binds to the membrane through at least two sites: a high-affinity site on the glycophorins2,10 and a site of lower… CONTINUE READING