Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861.
Cys-861 of mouse band 3 is equivalent to Cys-843 of human band 3, the only acylated cysteine residue in the anion exchanger AE1 of the red blood cell (Hamasaki et al. (1992) Progress Cell Res. 2, 65-71). Mutation of Cys-861 to serine or methionine caused no significant changes of band 3-mediated anion exchange as measured after expression of the appropriate cRNAs in Xenopus oocytes. Susceptibility to inhibition of transport by 4,4'-dinitrostilbene-2,2'-disulfonate and PCMBS was not affected. We conclude that palmitoylation is not an absolute requirement for the successful execution the anion transport function by the hydrophobic domain of band 3 in the plasma membrane.
Kang
D
D
Max Planck Institut für Biophysik, Frankfurt am Main, Germany.
Karbach
D
D
Passow
H
H
D000215:Acylation; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000838:Anions / Q000378:metabolism*; D001483:Base Sequence; D003545:Cysteine / Q000737:chemistry*; D018076:DNA, Complementary / Q000032:analysis; D008051:Lipid Bilayers / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D009865:Oocytes / Q000378:metabolism; D012313:RNA / Q000032:analysis; D014981:Xenopus
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D018076:DNA, Complementary; D008051:Lipid Bilayers; D012313:RNA; D003545:Cysteine