TY - JOUR
T1 - Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861
AU - Kang, Dongchon
AU - Karbach, Doris
AU - Passow, Hermann
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1994/9/14
Y1 - 1994/9/14
N2 - 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.
AB - 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.
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U2 - 10.1016/0005-2736(94)90317-4
DO - 10.1016/0005-2736(94)90317-4
M3 - Article
C2 - 7522566
AN - SCOPUS:0028017770
SN - 0005-2736
VL - 1194
SP - 341
EP - 344
JO - BBA - Biomembranes
JF - BBA - Biomembranes
IS - 2
ER -