Functional identification of protein phosphatase 1-binding consensus residues in NBCe1-B
DC Field | Value | Language |
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dc.contributor.author | Lee, Kyu Pil | - |
dc.contributor.author | Kim, Hyun Jin | - |
dc.contributor.author | Yang, Dongki | - |
dc.date.available | 2020-02-27T12:42:08Z | - |
dc.date.created | 2020-02-06 | - |
dc.date.issued | 2018-01 | - |
dc.identifier.issn | 1226-4512 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/4233 | - |
dc.description.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. | - |
dc.language | 영어 | - |
dc.language.iso | en | - |
dc.publisher | KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY | - |
dc.relation.isPartOf | KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY | - |
dc.subject | SODIUM-BICARBONATE COTRANSPORTER | - |
dc.subject | GUINEA-PIG PANCREAS | - |
dc.subject | INTERLOBULAR DUCTS | - |
dc.subject | CL-COTRANSPORTER | - |
dc.subject | WNK KINASES | - |
dc.subject | HCO3 | - |
dc.subject | TRANSPORTERS | - |
dc.subject | RECEPTOR | - |
dc.subject | IRBIT | - |
dc.subject | SPAK | - |
dc.title | Functional identification of protein phosphatase 1-binding consensus residues in NBCe1-B | - |
dc.type | Article | - |
dc.type.rims | ART | - |
dc.description.journalClass | 1 | - |
dc.identifier.wosid | 000422818400010 | - |
dc.identifier.doi | 10.4196/kjpp.2018.22.1.91 | - |
dc.identifier.bibliographicCitation | KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY, v.22, no.1, pp.91 - 99 | - |
dc.identifier.kciid | ART002308368 | - |
dc.identifier.scopusid | 2-s2.0-85041229761 | - |
dc.citation.endPage | 99 | - |
dc.citation.startPage | 91 | - |
dc.citation.title | KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY | - |
dc.citation.volume | 22 | - |
dc.citation.number | 1 | - |
dc.contributor.affiliatedAuthor | Yang, Dongki | - |
dc.type.docType | Article | - |
dc.subject.keywordAuthor | HCO3- secretion | - |
dc.subject.keywordAuthor | IRBIT | - |
dc.subject.keywordAuthor | NBCe1-B | - |
dc.subject.keywordAuthor | Protein phosphatase 1 | - |
dc.subject.keywordAuthor | SPAK | - |
dc.subject.keywordAuthor | WNK | - |
dc.subject.keywordPlus | SODIUM-BICARBONATE COTRANSPORTER | - |
dc.subject.keywordPlus | GUINEA-PIG PANCREAS | - |
dc.subject.keywordPlus | INTERLOBULAR DUCTS | - |
dc.subject.keywordPlus | CL-COTRANSPORTER | - |
dc.subject.keywordPlus | WNK KINASES | - |
dc.subject.keywordPlus | HCO3 | - |
dc.subject.keywordPlus | TRANSPORTERS | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | IRBIT | - |
dc.subject.keywordPlus | SPAK | - |
dc.relation.journalResearchArea | Pharmacology & Pharmacy | - |
dc.relation.journalResearchArea | Physiology | - |
dc.relation.journalWebOfScienceCategory | Pharmacology & Pharmacy | - |
dc.relation.journalWebOfScienceCategory | Physiology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
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