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Suh, Pann-Ghill
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dc.citation.endPage 804 -
dc.citation.number 4 -
dc.citation.startPage 793 -
dc.citation.title FEBS JOURNAL -
dc.citation.volume 273 -
dc.contributor.author Kim, E -
dc.contributor.author Lee, S -
dc.contributor.author Mian, MF -
dc.contributor.author Yun, SU -
dc.contributor.author Song, M -
dc.contributor.author Yi, KS -
dc.contributor.author Ryu, SH -
dc.contributor.author Suh, Pann-Ghill -
dc.date.accessioned 2023-12-22T10:08:32Z -
dc.date.available 2023-12-22T10:08:32Z -
dc.date.created 2014-09-02 -
dc.date.issued 2006-02 -
dc.description.abstract Vaults are highly conserved, ubiquitous ribonucleoprotein (RNP) particles with an unidentified function. For the three protein species (TEP1, VPARP, and MVP) and a small RNA that comprises vault, expression of the unique 100-kDa major vault protein (MVP) is sufficient to form the basic vault structure. q1To identify and characterize proteins that interact with the Src homology 2 (SH2) domain of Src and potentially regulate Src activity, we used a pull-down assay using GST-Src-SH2 fusion proteins. We found MVP as a Src-SH2 binding protein in human stomach tissue. Interaction of Src and MVP was also observed in 253J q2stomach cancer cells. A subcellular localization study using immunofluorescence microscopy shows that epidermal growth factor (EGF) stimulation triggers MVP translocation from the nucleus to the cytosol and perinuclear region where it colocalizes with Src. We found that the interaction between Src and MVP is critically dependent on Src activity and protein (MVP) tyrosyl phosphorylation, which are induced by EGF stimulation. Our results also indicate MVP to be a novel substrate of Src and phosphorylated in an EGF-dependent manner. Interestingly, purified MVP inhibited the in vitro tyrosine kinase activity of Src in a concentration-dependent manner. MVP overexpression downregulates EGF-dependent ERK activation in Src overexpressing cells. To our knowledge, this is the first report of MVP interacting with a protein tyrosine kinase involved in a distinct cell signalling pathway. It appears that MVP is a novel regulator of Src-mediated signalling cascades. -
dc.identifier.bibliographicCitation FEBS JOURNAL, v.273, no.4, pp.793 - 804 -
dc.identifier.doi 10.1111/j.1742-4658.2006.05112.x -
dc.identifier.issn 1742-464X -
dc.identifier.scopusid 2-s2.0-33644944176 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/5671 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=33644944176 -
dc.identifier.wosid 000234974600011 -
dc.language 영어 -
dc.publisher WILEY-BLACKWELL -
dc.title Crosstalk between Src and major vault protein in epidermal growth factor-dependent cell signalling -
dc.type Article -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordAuthor ERK signaling pathway -
dc.subject.keywordAuthor MVP -
dc.subject.keywordAuthor Src -
dc.subject.keywordAuthor Src activity -
dc.subject.keywordAuthor tyrosine phophorylation -
dc.subject.keywordPlus TYROSINE KINASES -
dc.subject.keywordPlus DRUG-RESISTANCE -
dc.subject.keywordPlus RIBONUCLEOPROTEIN-PARTICLES -
dc.subject.keywordPlus POLYACRYLAMIDE-GELS -
dc.subject.keywordPlus NIH 3T3-CELLS -
dc.subject.keywordPlus CANCER-CELL -
dc.subject.keywordPlus PHOSPHORYLATION -
dc.subject.keywordPlus ACTIVATION -
dc.subject.keywordPlus PP60C-SRC -
dc.subject.keywordPlus DISRUPTION -

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