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AHCYL2 (long‐IRBIT) as a potential regulator of the electrogenic Na + ‐HCO 3 − cotransporter NBCe1‐B
Author(s) -
Yamaguchi Soichiro,
Ishikawa Toru
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.12.036
Subject(s) - cotransporter , regulator , cytosol , intracellular , chemistry , microbiology and biotechnology , biophysics , yeast , immunoprecipitation , biochemistry , biology , sodium , enzyme , gene , organic chemistry
Although AHCYL2 (long‐IRBIT) is highly homologous to IRBIT, which regulates ion‐transporting proteins including the electrogenic Na + ‐HCO 3 − cotransporter NBCe1‐B, its functions are poorly understood. Here, we found that AHCYL2 interacts with NBCe1‐B in bovine parotid acinar cells using yeast two‐hybrid, immunofluorescence confocal microscopy and co‐immunoprecipitation analyses. Whole‐cell patch‐clamp experiments revealed that co‐expression of AHCYL2 reduces the apparent affinity for intracellular Mg 2+ in inhibition of NBCe1‐B currents specifically in a HCO 3 − ‐deficient cellular condition. Our data unveil AHCYL2 as a potential regulator of NBCe1‐B in mammalian cells. We propose that cytosolic ionic condition appropriate for AHCYL2 to function might be different from IRBIT.