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- W157050818 abstract "We have investigated the molecular basis for regulation of the ubiquitous AE2/SLC4A2 anion exchanger by intracellular pH (pHi) and extracellular pH (pHo) through mutagenesis of C-terminal transmembrane domain (TMD) amino acid residues not conserved in the closely related but pH-insensitive AE1/SLC4A1. Selected conserved residues were also studied. AE2-mediated Cl−/Cl− exchange was measured as DIDS-sensitive 36Cl− efflux from Xenopus oocytes by varying pHi at constant pHo, and by varying pHo at near-constant pHi. Mutation of all 26 non-conserved charged residues of the AE2 TMD yielded functional protein, but mutations of 4 conserved charged residues reduced or abolished function. Wt pHi-sensitivity of anion exchange was reduced upon individual mutation of AE2 TMD residues R921, F922, P1077 and R1107, whereas TMD mutants K1153R, R1155K, R1202L displayed enhanced sensitivity to acidic pHi. In addition, individual mutagenesis of non-conserved AE2 TMD residues E981, K982 and D1075 to the corresponding AE1 residues significantly acid-shifted pHo-sensitivity. These results demonstrate that multiple conserved charged residues are important for basal transport function of AE2. They further suggests that multiple non-contiguous TMD amino acid residues contribute to regulation of AE2 by pH, and highlight the complexity of the molecular mechanisms by which pH regulates bicarbonate transporters." @default.
- W157050818 created "2016-06-24" @default.
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- W157050818 date "2007-01-01" @default.
- W157050818 modified "2023-09-26" @default.
- W157050818 title "Nonconserved charged residues of the AE2 transmembrane domain alter regulation of anion exchange by pH" @default.
- W157050818 doi "https://doi.org/10.1096/fasebj.21.6.a1281-c" @default.
- W157050818 hasPublicationYear "2007" @default.
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