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

Dongchon Kang, Doris Karbach, Hermann Passow

Research output: Contribution to journalArticle

17 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)341-344
Number of pages4
JournalBBA - Biomembranes
Volume1194
Issue number2
DOIs
Publication statusPublished - Sep 14 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

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