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

First Author  Kopito RR Year  1989
Journal  Cell Volume  59
Issue  5 Pages  927-37
PubMed ID  2686841 Mgi Jnum  J:16498
Mgi Id  MGI:64573 Doi  10.1016/0092-8674(89)90615-6
Citation  Kopito RR, et al. (1989) Regulation of intracellular pH by a neuronal homolog of the erythrocyte anion exchanger. Cell 59(5):927-37
abstractText  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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