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DC Field | Value | Language |
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dc.citation.endPage | 227 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 216 | - |
dc.citation.title | EXPERIMENTAL AND MOLECULAR MEDICINE | - |
dc.citation.volume | 42 | - |
dc.contributor.author | Chung, Sang-Hee | - |
dc.contributor.author | Kim, Sung-Kuk | - |
dc.contributor.author | Kim, Jung Kuk | - |
dc.contributor.author | Yang, Yong-Ryoul | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Chang, Jong-Soo | - |
dc.date.accessioned | 2023-12-22T07:12:11Z | - |
dc.date.available | 2023-12-22T07:12:11Z | - |
dc.date.created | 2014-09-03 | - |
dc.date.issued | 2010-03 | - |
dc.description.abstract | Growth factor stimulation induces Y783 phosphorylation of phosphoinositide-specific PLC-γ1, and the subsequent activation of this enzyme in a cellular signaling cascade. Previously, we showed that a double point mutation, Y509A/F510A, of PLC-γ1, abolished interactions with translational elongation factor 1-α. Here, we report that the Y509A/F510A mutant PLC-γ1 displayed extremely high levels of Y783 phosphorylation and enhanced catalytic activity, compared to wild-type PLC-γ1, upon treatment of COS7 cells with EGF. In quiescent COS7 cells, the Y509A/F510A mutant PLC-γ1 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-γ1 (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-γ1, but no longer requires Y783 phosphorylation step for the Y509A/F510A mutant PLC-γ1 activation in vivo. | - |
dc.identifier.bibliographicCitation | EXPERIMENTAL AND MOLECULAR MEDICINE, v.42, no.3, pp.216 - 227 | - |
dc.identifier.doi | 10.3858/emm.2010.42.3.023 | - |
dc.identifier.issn | 1226-3613 | - |
dc.identifier.scopusid | 2-s2.0-77950534013 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5606 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77950534013 | - |
dc.identifier.wosid | 000276279800007 | - |
dc.language | 영어 | - |
dc.publisher | KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY | - |
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.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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