ANION TRANSPORT FUNCTION OF MOUSE ERYTHROID BAND-3 PROTEIN (AE1) DOESNOT 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 b lood cell (Hamasaki et al. (1992) Progress Cell Res. 2, 65-71). Mutati on of Cys-861 to serine or methionine caused no significant changes of band 3-mediated anion exchange as measured after expression of the ap propriate cRNAs in Xenopus oocytes. Susceptibility to inhibition of tr ansport by 4,4'-dinitrostilbene-2,2'-disulfonate and PCMBS was not aff ected. We conclude that palmitoylation is not an absolute requirement for the successful execution the anion transport function by the hydro phobic domain of band 3 in the plasma membrane.