Anion transport function of mouse erythroid band 3 protein (AE1) does not 
require acylation of cysteine residue 861

Kang, Dongchon; Karbach, Doris; Passow, Hermann

doi:10.1016/0005-2736(94)90317-4

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Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861

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Kang, Dongchon
Emeritusgroup Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Karbach, Doris
Emeritusgroup Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Passow, Hermann
Emeritusgroup Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Kang, D., Karbach, D., & Passow, H. (1994). Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861. Biochimica et Biophysica Acta-Biomembranes, 1194(2), 341-344. doi:10.1016/0005-2736(94)90317-4.

Cite as: https://hdl.handle.net/21.11116/0000-0008-32A0-A

Abstract

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.