title: Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3.
abstract: The cytoplasmic domain of band 3 serves as a center of erythrocyte membrane organization and constitutes the major substrate of erythrocyte tyrosine kinases. Tyrosine phosphorylation of band 3 is induced by several physiologic stimuli, including malaria parasite invasion, cell shrinkage, normal cell aging, and oxidant stress (thalassemias, sickle cell disease, glucose-6-phosphate dehydrogenase deficiency, etc). In an effort to characterize the biologic sequelae of band 3 tyrosine phosphorylation, we looked for changes in the polypeptide's function that accompany its phosphorylation. We report that tyrosine phosphorylation promotes dissociation of band 3 from the spectrin-actin skeleton as evidenced by: (1) a decrease in ankyrin affinity in direct binding studies, (2) an increase in detergent extractability of band 3 from ghosts, (3) a rise in band 3 cross-linkability by bis-sulfosuccinimidyl-suberate, (4) significant changes in erythrocyte morphology, and (5) elevation of the rate of band 3 diffusion in intact cells. Because release of band 3 from its ankyrin and adducin linkages to the cytoskeleton can facilitate changes in multiple membrane properties, tyrosine phosphorylation of band 3 is argued to enable adaptive changes in erythrocyte biology that permit the cell to respond to the above stresses.
authors.affiliation: Department of Genetics, Biology and Biochemistry, University of Turin, Turin, Italy.
authors.forename: Emanuela
authors.initials: E
authors.lastname: Ferru
authors.forename: Katie
authors.initials: K
authors.lastname: Giger
authors.forename: Antonella
authors.initials: A
authors.lastname: Pantaleo
authors.forename: Estela
authors.initials: E
authors.lastname: Campanella
authors.forename: Jesse
authors.initials: J
authors.lastname: Grey
authors.forename: Ken
authors.initials: K
authors.lastname: Ritchie
authors.forename: Rosa
authors.initials: R
authors.lastname: Vono
authors.forename: Francesco
authors.initials: F
authors.lastname: Turrini
authors.forename: Philip S
authors.initials: PS
authors.lastname: Low
mesh_terms: D000199:Actins / Q000378:metabolism; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D017487:Ankyrins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D003599:Cytoskeleton / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism*; D006801:Humans; D015151:Immunoblotting; D010766:Phosphorylation / Q000187:drug effects; D011485:Protein Binding; D014443:Tyrosine / Q000378:metabolism*; D014638:Vanadates / Q000494:pharmacology
chemical_list: D000199:Actins; D001457:Anion Exchange Protein 1, Erythrocyte; D017487:Ankyrins; D003432:Cross-Linking Reagents; D014638:Vanadates; D014443:Tyrosine