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International Journal of Cell Biology
Volume 2011, Article ID 136802, 8 pages
Review Article

Band 3 Missense Mutations and Stomatocytosis: Insight into the Molecular Mechanism Responsible for Monovalent Cation Leak

1Institut de Biologie du Développement et Cancer, UMR6543, CNRS, 28 Avenue Valrose, 06108 Nice Cedex 2, France
2Institut de Biologie du Développement et Cancer, Université de Nice, 06108 Nice Cedex 2, France

Received 6 April 2011; Revised 27 May 2011; Accepted 29 May 2011

Academic Editor: Lars Kaestner

Copyright © 2011 Damien Barneaud-Rocca et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Missense mutations in the erythroid band 3 protein (Anion Exchanger 1) have been associated with hereditary stomatocytosis. Features of cation leaky red cells combined with functional expression of the mutated protein led to the conclusion that the AE1 point mutations were responsible for N a + and K + leak through a conductive mechanism. A molecular mechanism explaining mutated AE1-linked stomatocytosis involves changes in AE1 transport properties that become leaky to N a + and K + . However, another explanation suggests that point-mutated AE1 could regulate a cation leak through other transporters. This short paper intends to discuss these two alternatives.