Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870546 | FEBS Letters | 2014 | 6 Pages |
Abstract
Although AHCYL2 (long-IRBIT) is highly homologous to IRBIT, which regulates ion-transporting proteins including the electrogenic Na+-HCO3â 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 Mg2+ in inhibition of NBCe1-B currents specifically in a HCO3â-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.
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Authors
Soichiro Yamaguchi, Toru Ishikawa,