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Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger.
Department of Biological Sciences, Stanford University, California 94305-5020.
We have isolated AE3, a novel gene expressed primarily in brain neurons and in heart. The predicted AE3 polypeptide shares a high degree of identity with the anion exchange and cytoskeletal binding domains of the erythrocyte band 3 protein. Expression of AE3 cDNA in COS cells leads to chronic cytoplasmic acidification and to chloride- and bicarbonate-dependent changes in intracellular pH, confirming that this gene product is an anion exchanger. Characterization of an AE3 mutant lacking the NH2-terminal 645 amino acids demonstrates that the COOH-terminal half of the polypeptide is both necessary and sufficient for correct insertion into the plasma membrane and for anion exchange activity. The NH2-terminal domain may play a role in regulating the activity of the exchanger and may be involved in the structural organization of the cytoskeleton in neurons.
PMID: 2686841 [PubMed - indexed for MEDLINE]
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Cited by 20 PubMed Central articles
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Acute regulation of mouse AE2 anion exchanger requires isoform-specific amino acid residues from most of the transmembrane domain.
Stewart AK, Kurschat CE, Vaughan-Jones RD, Shmukler BE, Alper SL.
J Physiol. 2007 Oct 1; 584(Pt 1):59-73. Epub 2007 Aug 9.
[J Physiol. 2007]
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Mice with a targeted disruption of the Cl-/HCO3- exchanger AE3 display a reduced seizure threshold.
Hentschke M, Wiemann M, Hentschke S, Kurth I, Hermans-Borgmeyer I, Seidenbecher T, Jentsch TJ, Gal A, Hübner CA.
Mol Cell Biol. 2006 Jan; 26(1):182-91.
[Mol Cell Biol. 2006]
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Critical amino acid residues involved in the electrogenic sodium-bicarbonate cotransporter kNBC1-mediated transport.
Abuladze N, Azimov R, Newman D, Sassani P, Liu W, Tatishchev S, Pushkin A, Kurtz I.
J Physiol. 2005 Jun 15; 565(Pt 3):717-30. Epub 2005 Apr 7.
[J Physiol. 2005]
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