Dual Transport Properties of Anion Exchanger 1
THE SAME TRANSMEMBRANE SEGMENT IS INVOLVED IN ANION EXCHANGE AND IN A CATION LEAK
- From the Institut de Biologie du Développement et Cancer, UMR6543 Université de Nice-Centre National de la Recherche Scientifique, 28 avenue Valrose, 06108 Nice cedex 2, France
- 1 To whom correspondence should be addressed: IBDC, Bâtiment de Sciences naturelles, 28 av. Valrose, 06108 Nice cedex 2, France. E-mail: guizouar{at}unice.fr.
Abstract
Previous results suggested that specific point mutations in human anion exchanger 1 (AE1) convert the electroneutral anion exchanger into a monovalent cation conductance. In the present study, the transport site for anion exchange and for the cation leak has been studied by cysteine scanning mutagenesis and sulfhydryl reagent chemistry. Moreover, the role of some highly conserved amino acids within members of the SLC4 family to which AE1 belongs has been assessed in AE1 transport properties. The results suggest that the same transport site within the AE1 spanning domain is involved in anion exchange or in cation transport. A functioning mechanism for this transport site is proposed according to transport properties of the different studied point mutations of AE1.
- Chloride Transport
- Erythrocyte
- Membrane Proteins
- Potassium Transport
- Sodium Transport
- AE1
- Anion Exchanger
- Band 3
- SLC4A1
Footnotes
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The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. 1.
- Received July 21, 2010.
- Revision received January 19, 2011.
- © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
