Acute regulation of mouse AE2 anion exchanger requires isoform-specific amino acid residues from most of the transmembrane domain.

Journal article

The widely expressed anion exchanger polypeptide AE2/SLC4A2 is acutely inhibited by acidic intracellular (pH(i)), by acidic extracellular pH (pH(o)), and by the calmodulin inhibitor, calmidazolium, whereas it is acutely activated by NH(4)(+). The homologous erythroid/kidney AE1/SLC4A1 polypeptide is insensitive to these regulators. Each of these AE2 regulatory responses requires the presence of AE2's C-terminal transmembrane domain (TMD). We have now measured (36)Cl(-) efflux from Xenopus ooc...

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Authors: Stewart, A; Kurschat, C; Vaughan-Jones, R; Shmukler, B; Alper, S

• Publication status: Published
• Journal: Journal of physiology
• Volume: 584
• Issue: Pt 1
• Pages: 59-73
• Publication date: 2007-10-01
• DOI: 10.1113/jphysiol.2007.136119
• EISSN: 1469-7793
• ISSN: 0022-3751
• Language: English
• Keywords: Quaternary Ammonium Compounds; Protein Structure, Tertiary; Imidazoles; Antiporters; Xenopus laevis; Female; Hydrogen-Ion Concentration; Recombinant Fusion Proteins; Animals; Codon, Nonsense; Anion Exchange Protein 1, Erythrocyte; Oocytes; Anion Transport Proteins; Protein Isoforms; Cell Membrane; Mice; Amino Acid Sequence; Peptides