Functional identification of protein phosphatase 1-binding consensus residues in NBCe1-B
The Korean Journal of Physiology and Pharmacology
;
: 91-99, 2018.
Artigo
em Inglês
| 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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Transdução de Sinais
/
Mutagênese Sítio-Dirigida
/
Domínio Catalítico
/
Consenso
/
Imunoprecipitação
/
Proteína Fosfatase 1
/
Aminoácidos
/
Concentração de Íons de Hidrogênio
Tipo de estudo:
Estudo diagnóstico
/
Guia de Prática Clínica
Idioma:
Inglês
Revista:
The Korean Journal of Physiology and Pharmacology
Ano de publicação:
2018
Tipo de documento:
Artigo
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