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

Damien Barneaud-Rocca | Zendy; Bernard Pellissier | Zendy; Franck Borgèse | Zendy; Hélène Guizouarn | Zendy

Open Access

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

Author(s) -

Damien Barneaud-Rocca,

Bernard Pellissier,

Franck Borgèse,

Hélène Guizouarn

Publication year - 2011

Publication title -

international journal of cell biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.587

H-Index - 53

eISSN - 1687-8884

pISSN - 1687-8876

DOI - 10.1155/2011/136802

Subject(s) - missense mutation , point mutation , band 3 , leak , mechanism (biology) , glycophorin , mutation , microbiology and biotechnology , chemistry , genetics , biochemistry , biophysics , biology , membrane protein , gene , physics , membrane , quantum mechanics , thermodynamics

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 Na + 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 Na + 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.

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