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  • Title: Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger.
    Author: Kopito RR, Lee BS, Simmons DM, Lindsey AE, Morgans CW, Schneider K.
    Journal: Cell; 1989 Dec 01; 59(5):927-37. PubMed ID: 2686841.
    Abstract:
    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.
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