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

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.

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 Creators:
Kang, Dongchon1, Author           
Karbach, Doris1, Author           
Passow, Hermann1, Author           
Affiliations:
1Emeritusgroup Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_3273412              

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Free keywords: Chloride transport; Palmitoylation; Site-directed mutagenesis; Oocyte; (Xenopus)
 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.

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Language(s): eng - English
 Dates: 1994-03-101994-09-14
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/0005-2736(94)90317-4
PMID: 7522566
 Degree: -

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Title: Biochimica et Biophysica Acta-Biomembranes
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1194 (2) Sequence Number: - Start / End Page: 341 - 344 Identifier: ISSN: 0005-2736
CoNE: https://pure.mpg.de/cone/journals/resource/954926938702