title: Control of band 3 lateral and rotational mobility by band 4.2 in intact erythrocytes: release of band 3 oligomers from low-affinity binding sites.
abstract: Band 4.2 is a human erythrocyte membrane protein of incompletely characterized structure and function. Erythrocytes deficient in band 4.2 protein were used to examine the functional role of band 4.2 in intact erythrocyte membranes. Both the lateral and the rotational mobilities of band 3 were increased in band 4.2-deficient erythrocytes compared to control cells. In contrast, the lateral mobility of neither glycophorins nor a fluorescent phospholipid analog was altered in band 4.2-deficient cells. Compared to controls, band 4.2-deficient erythrocytes manifested a decreased ratio of band 3 to spectrin, and band 4.2-deficient membrane skeletons had decreased extractability of band 3 under low-salt conditions. Normal band 4.2 was found to bind to spectrin in solution and to promote the binding of spectrin to ankyrin-stripped inside-out vesicles. We conclude that band 4.2 provides low-affinity binding sites for both band 3 oligomers and spectrin dimers on the human erythrocyte membrane. Band 4.2 may serve as an accessory linking protein between the membrane skeleton and the overlying lipid bilayer.
authors.affiliation: Department of Biological Chemistry, Harvard Medical School, Boston, Massachusetts 02115, USA. degolan@warren.med.harvard.edu
authors.forename: D E
authors.initials: DE
authors.lastname: Golan
authors.forename: J D
authors.initials: JD
authors.lastname: Corbett
authors.forename: C
authors.initials: C
authors.lastname: Korsgren
authors.forename: H S
authors.initials: HS
authors.lastname: Thatte
authors.forename: S
authors.initials: S
authors.lastname: Hayette
authors.forename: Y
authors.initials: Y
authors.lastname: Yawata
authors.forename: C M
authors.initials: CM
authors.lastname: Cohen
mesh_terms: D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry*; D001665:Binding Sites; D055592:Biophysical Phenomena; D001703:Biophysics; D001798:Blood Proteins / Q000737:chemistry*; D003598:Cytoskeletal Proteins; D004910:Erythrocyte Membrane / Q000737:chemistry*; D006801:Humans; D066298:In Vitro Techniques; D008565:Membrane Proteins / Q000737:chemistry*; D009038:Motion; D011487:Protein Conformation; D012399:Rotation; D013049:Spectrin / Q000737:chemistry
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; C044791:erythrocyte membrane band 4.2 protein; D013049:Spectrin