DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, HY | - |
dc.contributor.author | Park, JB | - |
dc.contributor.author | Jang, IH | - |
dc.contributor.author | Chae, YC | - |
dc.contributor.author | Kim, JH | - |
dc.contributor.author | Kim, IS | - |
dc.contributor.author | Suh, PG | - |
dc.contributor.author | Ryu, SH | - |
dc.date.accessioned | 2016-03-31T12:30:25Z | - |
dc.date.available | 2016-03-31T12:30:25Z | - |
dc.date.created | 2009-02-28 | - |
dc.date.issued | 2004-01 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.other | 2004-OAK-0000004174 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/17983 | - |
dc.description.abstract | Mammalian phospholipase D (PLD) has been reported to be a key enzyme for epidermal growth factor (EGF)induced cellular signaling, however, the regulatory mechanism of PLD is still unclear. In this report, we found that Munc-18-1 is a potent negative regulator of PLD in the basal state and that its inhibition is abolished by EGF stimulation. We investigated PLD-binding proteins obtained from rat brain extract, and identified a 67-kDa protein as Munc-18-1 by peptide-mass fingerprinting. The direct association between PLD and Munc-18-1 was confirmed by in vitro binding analysis using the purified proteins, and their binding sites were identified as the phox homology domain of PLD and multiple sites of Munc-18-1. PLD activity was potently inhibited by Munc-18-1 in vitro (IC50 = 2 - 5 nM), and the cotransfection of COS-7 cells with Munc-18-1 and PLD inhibited basal PLD activity in vivo. In the basal state, Munc-18-1 coprecipitated with PLD and colocalized with PLD2 at the plasma membrane of COS-7 cells. EGF treatment triggered the dissociation of Munc-18-1 from PLD when PLD was activated by EGF. The dissociation of the endogenous interaction between Munc-18-1 and PLD, and the activation of PLD by EGF were also observed in primary cultured chromaffin cells. These results suggest that Munc-18-1 is a potent negative regulator of basal PLD activity and that EGF stimulation abolishes this interaction. | - |
dc.description.statementofresponsibility | X | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLO | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.title | Munc-18-1 inhibits phospholipase D activity by direct interaction in an epidermal growth factor-reversible manner | - |
dc.type | Article | - |
dc.contributor.college | 생명과학과 | - |
dc.identifier.doi | 10.1074/JBC.M310976200 | - |
dc.author.google | Lee, HY | - |
dc.author.google | Park, JB | - |
dc.author.google | Jang, IH | - |
dc.author.google | Chae, YC | - |
dc.author.google | Kim, JH | - |
dc.author.google | Kim, IS | - |
dc.author.google | Suh, PG | - |
dc.author.google | Ryu, SH | - |
dc.relation.volume | 279 | - |
dc.relation.issue | 16 | - |
dc.relation.startpage | 16339 | - |
dc.relation.lastpage | 16348 | - |
dc.contributor.id | 10052640 | - |
dc.relation.journal | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.relation.index | SCI급, SCOPUS 등재논문 | - |
dc.relation.sci | SCI | - |
dc.collections.name | Journal Papers | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.279, no.16, pp.16339 - 16348 | - |
dc.identifier.wosid | 000220747900080 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 16348 | - |
dc.citation.number | 16 | - |
dc.citation.startPage | 16339 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 279 | - |
dc.contributor.affiliatedAuthor | Suh, PG | - |
dc.contributor.affiliatedAuthor | Ryu, SH | - |
dc.identifier.scopusid | 2-s2.0-1942469382 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 23 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | ARTICLE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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