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The abundant membrane protein AE1 normally functions as an obligate anion exchanger, with classical carrier properties, in human red blood cells. Recently, four single point mutations of hAE1 have been identified that have lost the anion exchange function, and act as non-selective monovalent cation channels, as shown in both red cell flux and oocyte expression studies. The red cell transport function shows a paradoxical temperature dependence, and is associated with spherocytic and stomatocytic red cell defects, and haemolytic anaemias. Other forms of AE1, including the native AE1 in trout red cells, and the human mutation R760Q show both channel-like and anion exchange properties. The present results point to membrane domains 9 and 10 being important in the functional modification of AE1 activity.

Original publication

DOI

10.1098/rstb.2008.0154

Type

Journal article

Journal

Philos Trans R Soc Lond B Biol Sci

Publication Date

27/01/2009

Volume

364

Pages

189 - 194

Keywords

Anion Exchange Protein 1, Erythrocyte, Cations, Mutation, Protein Conformation