Functional identification of protein phosphatase 1-binding consensus residues in NBCe1-B
The Korean Journal of Physiology and Pharmacology
;
: 91-99, 2018.
Article
in English
| WPRIM
| ID: wpr-727934
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Signal Transduction
/
Mutagenesis, Site-Directed
/
Catalytic Domain
/
Consensus
/
Immunoprecipitation
/
Protein Phosphatase 1
/
Amino Acids
/
Hydrogen-Ion Concentration
Type of study:
Diagnostic study
/
Practice guideline
Language:
English
Journal:
The Korean Journal of Physiology and Pharmacology
Year:
2018
Type:
Article
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