Erythrocyte band 3 protein strongly interacts with phosphoinositides

FEBS Letters

Maretzki, Dieter¹  Hanicak, Andreas⁵  Visser, Antonie J.W.G.²  Pap, Eward²  Schubert, Dieter⁵  Wirtz, Karel W.A.⁴  Reimann, Barbara³ 

[1] Institutes of Medical Physics/Biophysics, Charité, Humboldt University, D-10098 Berlin, Germany;Department of Biochemistry, Agricultural University, NL-6703 HA Wageningen, The Netherlands;Institutes of Biochemistry, Charité, Humboldt University, D-10098 Berlin, Germany;Centre for Biomembranes and Lipid Enzymology, Utrecht University, NL-3584 CH Utrecht, The Netherlands;Biophysics Institute, J.W. Goethe University, Theodor-Stern-Kai 7, Haus 74, D-60590 Frankfurt am Main, Germany

关键词: Band 3 protein;    Phosphoinositide;    Protein—lipid association;    Erythrocyte membrane;    C12E9;    nonaethyleneglycol lauryl ether;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PG;    phosphatidylglycerol;    PI;    phospatidylinositol;    PIP;    phosphatidylinositol 4-phosphate;    PIP2;    phosphatidylinositol 4;    5-bisphosphate;    PS;    phosphatidylserine;    SM;    sphingomyelin;   

DOI  :  10.1016/0014-5793(94)00595-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

85% of the phosphorus coisolated with band 3 protein during separation of the intrinsic proteins of the human erythrocyte membrane by zonal electrophoresis in high concentrations of acetic acid was found to be derived from phosphoinositides, mainly phosphatidylinositol 4,5-bisphosphate. When native band 3 protein and pyrene-labelled phospholipids were present in micelles of the nonionic detergent nonaethyleneglycol lauryl ether, strong resonance energy transfer was observed between the tryptophan residues and phosphatidylinositol 4,5-bisphosphate and, to a smaller degree, phosphatidylinositol 4-phosphate. We conclude that band 3 protein strongly interacts with phosphoinositides, in particular with phosphatidylinositol 4,5-bisphosphate.

【 授权许可】

Unknown