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EGFR phosphorylation-dependent formation of cell-cell contacts by Ras/Erks cascade inhibition

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dc.contributor.authorKang, Eun-Sil-
dc.contributor.authorOh, Min-A-
dc.contributor.authorLee, Sin-Ae-
dc.contributor.authorKim, Tae Young-
dc.contributor.authorKim, Sung-Hoon-
dc.contributor.authorGotoh, Noriko-
dc.contributor.authorKim, Yong-Nyun-
dc.contributor.authorLee, Jung Weon-
dc.creator이정원-
dc.date.accessioned2013-04-16T07:52:33Z-
dc.date.available2013-04-16T07:52:33Z-
dc.date.issued2007-06-
dc.identifier.citationBIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH Vol.1773 No.6, pp. 833-843-
dc.identifier.issn0167-4889-
dc.identifier.urihttp://hdl.handle.net/10371/82051-
dc.description.abstractCell-cell contacts play important roles in the homeostasis of normal epithelium and in the steps of metastasis of tumor cells, although signaling mechanisms to regulate cell-cell contacts are unclear. In this study, we observed that phenotype of no cell-cell contacts in rat intestinal epithelial cell subline (RIE1-Sca) correlated with increased Erk1/2 signaling activity, compared to that of parental RIE1 cells growing in colonies. Furthermore, cell-cell contacts between RIE1-Sca cells were reformed by treatment with a specific MEK inhibitor (U0126), with translocation of ZO1 and beta-catenin to cell-cell contacts, without changes of their expression levels. U0126 treatment also increased EGFR phosphorylation in a ligand-independent manner. Pretreatment with EGFR kinase inhibitor abolished U0126 treatment-mediated EGFR phosphorylation, and expression of dominant negative H-Ras N17 allowed EGFR phosphorylation and cell-cell contacts even without U0126 treatment. Furthermore, the expression of a nonphosphorylatable EGFR Y5F mutant abolished U0126-mediated cell-cell contacts. U0126 treatment also caused less efficient wound healing by keeping monolayer integrity intact, compared to control untreated cells. This U0126-mediated reduction in wound healing was further altered either by pretreatment of EGFR kinase inhibitor or expression of H-Ras N17 or EGFR Y517. Taken together, this study supports a unique mechanism of cell-cell contact formation through MEK/Erks inhibition-mediated EGFR phosphorylation. (c) 2007 Elsevier B.V. All rights reserved.en
dc.language.isoenen
dc.publisherELSEVIERen
dc.subject복합학en
dc.subjectcell-cell contacten
dc.subjectErk-
dc.subjectRas-
dc.subjectEGFR-
dc.subject신호전달-
dc.titleEGFR phosphorylation-dependent formation of cell-cell contacts by Ras/Erks cascade inhibitionen
dc.typeArticle-
dc.contributor.AlternativeAuthor강은실-
dc.contributor.AlternativeAuthor오민아-
dc.contributor.AlternativeAuthor이신애-
dc.contributor.AlternativeAuthor김태영-
dc.contributor.AlternativeAuthor김성훈-
dc.contributor.AlternativeAuthor김용년-
dc.contributor.AlternativeAuthor이정원-
dc.identifier.doi10.1016/j.bbamcr.2007.02.003-
dc.description.srndOAIID:oai:osos.snu.ac.kr:snu2007-01/102/0000003910/2-
dc.description.srndSEQ:2-
dc.description.srndPERF_CD:SNU2007-01-
dc.description.srndEVAL_ITEM_CD:102-
dc.description.srndUSER_ID:0000003910-
dc.description.srndADJUST_YN:Y-
dc.description.srndEMP_ID:A078142-
dc.description.srndDEPT_CD:375-
dc.description.srndCITE_RATE:4.374-
dc.description.srndFILENAME:35KES_BBA.pdf-
dc.description.srndDEPT_NM:약학과-
dc.description.srndEMAIL:jwl@snu.ac.kr-
dc.description.srndCONFIRM:Y-
dc.identifier.rimsid3446-
dc.identifier.srnd2007-01/102/0000003910/2-
dc.type.rimsART-
Appears in Collections:
College of Pharmacy (약학대학)Dept. of Pharmacy (약학과)Journal Papers (저널논문_약학과)
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