Functional identification of protein phosphatase 1-binding consensus residues in NBCe1-B
- Authors
- Lee, Kyu Pil; Kim, Hyun Jin; Yang, Dongki
- Issue Date
- Jan-2018
- Publisher
- KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY
- Keywords
- HCO3- secretion; IRBIT; NBCe1-B; Protein phosphatase 1; SPAK; WNK
- Citation
- KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY, v.22, no.1, pp.91 - 99
- Journal Title
- KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY
- Volume
- 22
- Number
- 1
- Start Page
- 91
- End Page
- 99
- URI
- https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/4233
- DOI
- 10.4196/kjpp.2018.22.1.91
- ISSN
- 1226-4512
- Abstract
- Protein phosphatase 1 (PP1) is involved in various signal transduction mechanisms as an extensive regulator. The PP1 catalytic subunit (PP1c) recognizes and binds to PP1-binding consensus residues (FxxR/KxR/K) in NBCe1-B. Consequently, we focused on identifying the function of the PP1-binding consensus residue, 922FMDRLK927, in NBCe1-B. Using site-directed mutagenesis and co-immunoprecipitation assays, we revealed that in cases where the residues were substituted (F922A, R925A, and K927A) or deleted (deletion of amino acids 922-927), NBCe1-B mutants inhibited PP1 binding to NBCe1-B. Additionally, by recording the intracellular pH, we found that PP1-binding consensus residues in NBCe1-B were not only critical for NBCe1-B activity, but also relevant to its surface expression level. Therefore, we reported that NBCe1-B, as a substrate of PP1, contains these residues in the C-terminal region and that the direct interaction between NBCe1-B and PP1 is functionally critical in controlling the regulation of the HCO3- transport. These results suggested that like IRBIT, PP1 was another novel regulator of HCO3- secretion in several types of epithelia.
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