DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, JK | - |
dc.contributor.author | Kwon, O | - |
dc.contributor.author | Kim, J | - |
dc.contributor.author | Kim, EK | - |
dc.contributor.author | Park, HK | - |
dc.contributor.author | Lee, JE | - |
dc.contributor.author | Kim, KL | - |
dc.contributor.author | Choi, JW | - |
dc.contributor.author | Lim, S | - |
dc.contributor.author | Seok, H | - |
dc.contributor.author | Lee-Kwon, W | - |
dc.contributor.author | Choi, JH | - |
dc.contributor.author | Kang, BH | - |
dc.contributor.author | Kim, S | - |
dc.contributor.author | Ryu, SH | - |
dc.contributor.author | Suh, PG | - |
dc.date.accessioned | 2016-04-01T08:12:42Z | - |
dc.date.available | 2016-04-01T08:12:42Z | - |
dc.date.created | 2012-08-09 | - |
dc.date.issued | 2012-06-15 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.other | 2012-OAK-0000026245 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/27477 | - |
dc.description.abstract | Phospholipase C-beta(PLC-beta) is a key molecule in G protein-coupled receptor (GPCR)-mediated signaling. Many studies have shown that the four PLC-beta subtypes have different physiological functions despite their similar structures. Because the PLC-beta subtypes possess different PDZ-binding motifs, they have the potential to interact with different PDZ proteins. In this study, we identified PDZ domain-containing 1 (PDZK1) as a PDZ protein that specifically interacts with PLC-beta 3. To elucidate the functional roles of PDZK1, we next screened for potential interacting proteins of PDZK1 and identified the somatostatin receptors (SSTRs) as another protein that interacts with PDZK1. Through these interactions, PDZK1 assembles as a ternary complex with PLC-beta 3 and SSTRs. Interestingly, the expression of PDZK1 and PLC-beta 3, but not PLC-beta 1, markedly potentiated SST-induced PLC activation. However, disruption of the ternary complex inhibited SST-induced PLC activation, which suggests that PDZK1-mediated complex formation is required for the specific activation of PLC-beta 3 by SST. Consistent with this observation, the knockdown of PDZK1 or PLC-beta 3, but not that of PLC-beta 1, significantly inhibited SST-induced intracellular Ca2+ mobilization, which further attenuated subsequent ERK1/2 phosphorylation. Taken together, our results strongly suggest that the formation of a complex between SSTRs, PDZK1, and PLC-beta 3 is essential for the specific activation of PLC-beta 3 and the subsequent physiologic responses by SST. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.title | PDZ Domain-containing 1 (PDZK1) Protein Regulates Phospholipase C-beta 3 (PLC-beta 3)-specific Activation of Somatostatin by Forming a Ternary Complex with PLC-beta 3 and Somatostatin Receptors | - |
dc.type | Article | - |
dc.contributor.college | 융합생명공학부 | - |
dc.identifier.doi | 10.1074/jbc.M111.337865 | - |
dc.author.google | Kim J.K., Kwon O., Kim J., Kim E.-K., Park H.K., Lee J.E., Kim K.L., Choi J.W., Lim S., Seok H., Lee-Kwon W., Choi J.H., Kang B.H., Kim S., Ryu S.H., Suh P.-G. | - |
dc.relation.volume | 287 | - |
dc.relation.issue | 25 | - |
dc.relation.startpage | 21012 | - |
dc.relation.lastpage | 21024 | - |
dc.contributor.id | 10069853 | - |
dc.relation.journal | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.287, no.25, pp.21012 - 21024 | - |
dc.identifier.wosid | 000306416800023 | - |
dc.date.tcdate | 2019-02-01 | - |
dc.citation.endPage | 21024 | - |
dc.citation.number | 25 | - |
dc.citation.startPage | 21012 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 287 | - |
dc.contributor.affiliatedAuthor | Kim, S | - |
dc.contributor.affiliatedAuthor | Ryu, SH | - |
dc.identifier.scopusid | 2-s2.0-84862271827 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 14 | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | C-BETA | - |
dc.subject.keywordPlus | SIGNAL-TRANSDUCTION | - |
dc.subject.keywordPlus | INTRINSIC DISORDER | - |
dc.subject.keywordPlus | SCAFFOLD PROTEINS | - |
dc.subject.keywordPlus | ACID SEQUENCES | - |
dc.subject.keywordPlus | BINDING SITES | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | ISOZYMES | - |
dc.subject.keywordPlus | HORMONE | - |
dc.subject.keywordPlus | INAD | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
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