Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger

Ron R. Kopito, Beth S. Lee, Donna M. Simmons, Ann E. Lindsey, Catherine W. Morgans, Karin Schneider

    Research output: Contribution to journalArticle

    194 Scopus citations

    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.

    Original languageEnglish (US)
    Pages (from-to)927-937
    Number of pages11
    JournalCell
    Volume59
    Issue number5
    DOIs
    StatePublished - Dec 1 1989

    ASJC Scopus subject areas

    • Biochemistry, Genetics and Molecular Biology(all)

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    Kopito, R. R., Lee, B. S., Simmons, D. M., Lindsey, A. E., Morgans, C. W., & Schneider, K. (1989). Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger. Cell, 59(5), 927-937. https://doi.org/10.1016/0092-8674(89)90615-6