DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chung, SH | - |
dc.contributor.author | Kim, SK | - |
dc.contributor.author | Kim, JK | - |
dc.contributor.author | Yang, YR | - |
dc.contributor.author | Suh, PG | - |
dc.contributor.author | Chang, JS | - |
dc.date.accessioned | 2015-06-25T01:56:13Z | - |
dc.date.available | 2015-06-25T01:56:13Z | - |
dc.date.created | 2010-04-23 | - |
dc.date.issued | 2010-03-31 | - |
dc.identifier.issn | 1226-3613 | - |
dc.identifier.other | 2015-OAK-0000020646 | en_US |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/10203 | - |
dc.description.abstract | Growth factor stimulation induces Y783 phosphorylation of phosphoinositide-specific PLC-gamma 1, and the subsequent activation of this enzyme in a cellular signaling cascade. Previously, we showed that a double point mutation, Y509A/F510A, of PLC-gamma 1, abolished interactions with translational elongation factor 1-alpha. Here, we report that the Y509A/F510A mutant PLC-gamma 1 displayed extremely high levels of Y783 phosphorylation and enhanced catalytic activity, compared to wild-type PLC-gamma 1, upon treatment of COS7 cells with EGF. In quiescent COS7 cells, the Y509A/F510A mutant PLC-gamma 1 exhibited a constitutive hydrolytic activity, whereas the wild-type counterpart displayed a basal level of activity. Upon treatment of COS7 cells with EGF, the Y783F mutation in Y509A/F510A PLC-gamma 1 (Y509A/F510A/Y783F triple mutant) cells also led to an enhanced catalytic activity, whereas Y783F mutation alone displayed a basal level of activity. Our results collectively suggest that the Y509A/F510A mutant is more susceptible to receptor tyrosine kinase-induced Y783 phosphorylation than is wild-type PLC-gamma 1, but no longer requires Y783 phosphorylation step for the Y509A/F510A mutant PLC-gamma 1 activation in vivo. | - |
dc.description.statementofresponsibility | open | en_US |
dc.language | English | - |
dc.publisher | KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY | - |
dc.relation.isPartOf | EXPERIMENTAL AND MOLECULAR MEDICINE | - |
dc.rights | BY_NC_ND | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/2.0/kr | en_US |
dc.title | A double point mutation in PCL-gamma 1 (Y509A/F510A) enhances Y783 phosphorylation and inositol phospholipid-hydrolyzing activity upon EGF stimulation | - |
dc.type | Article | - |
dc.contributor.college | 융합생명공학부 | en_US |
dc.identifier.doi | 10.3858/EMM.2010.42.3.023 | - |
dc.author.google | Chung, Sang-Hee | en_US |
dc.author.google | Kim, Sung-Kuk | en_US |
dc.author.google | Chang, Jong-Soo | en_US |
dc.author.google | Suh, Pann-Ghill | en_US |
dc.author.google | Yang, Yong-Ryoul | en_US |
dc.author.google | Kim, Jung Kuk | en_US |
dc.relation.volume | 42 | en_US |
dc.relation.issue | 3 | en_US |
dc.relation.startpage | 216 | en_US |
dc.relation.lastpage | 222 | en_US |
dc.contributor.id | 10052640 | en_US |
dc.relation.journal | EXPERIMENTAL AND MOLECULAR MEDICINE | en_US |
dc.relation.index | SCI급, SCOPUS 등재논문 | en_US |
dc.relation.sci | SCI | en_US |
dc.collections.name | Journal Papers | en_US |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | EXPERIMENTAL AND MOLECULAR MEDICINE, v.42, no.3, pp.216 - 222 | - |
dc.identifier.wosid | 000276279800007 | - |
dc.date.tcdate | 2019-01-01 | - |
dc.citation.endPage | 222 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 216 | - |
dc.citation.title | EXPERIMENTAL AND MOLECULAR MEDICINE | - |
dc.citation.volume | 42 | - |
dc.contributor.affiliatedAuthor | Suh, PG | - |
dc.identifier.scopusid | 2-s2.0-77950534013 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.wostc | 3 | - |
dc.description.scptc | 3 | * |
dc.date.scptcdate | 2018-10-274 | * |
dc.type.docType | Article | - |
dc.subject.keywordPlus | PLECKSTRIN HOMOLOGY DOMAINS | - |
dc.subject.keywordPlus | C-GAMMA | - |
dc.subject.keywordPlus | PH DOMAIN | - |
dc.subject.keywordPlus | TYROSINE RESIDUES | - |
dc.subject.keywordPlus | C-GAMMA-1 | - |
dc.subject.keywordPlus | GROWTH | - |
dc.subject.keywordPlus | PHOSPHOLIPASE-C-GAMMA-1 | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | C-BETA(2) | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordAuthor | phosphatidylinositol 4,5-bisphosphate | - |
dc.subject.keywordAuthor | phospholipase C gamma | - |
dc.subject.keywordAuthor | protein-tyrosine kinases | - |
dc.subject.keywordAuthor | src homology domains | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Medicine, Research & Experimental | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Research & Experimental Medicine | - |
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