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EGFR-c-Src-Mediated HDAC3 Phosphorylation Exacerbates Invasion of Breast Cancer Cells

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dc.contributor.author윤호근-
dc.contributor.author이승현-
dc.date.accessioned2022-08-19T06:23:40Z-
dc.date.available2022-08-19T06:23:40Z-
dc.date.issued2019-08-
dc.identifier.issn2073-4409-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/189129-
dc.description.abstractBreast cancer is one of the leading causes of morbidity and mortality among women. Epidermal growth factor receptor (EGFR) and proto-oncogene tyrosine-protein kinase Src (c-Src) are critical components of the signaling pathways that are associated with breast cancer. However, the regulatory mechanism of histone deacetylase 3 (HDAC3) in these pathways remains unclear. Using the Net Phos 3.1 program for the analysis of kinase consensus motifs, we found two c-Src-mediated putative phosphorylation sites, tyrosine (Tyr, Y)-328 and Y331 on HDAC3, and generated a phospho-specific HDAC3 antibody against these sites. c-Src-mediated phosphorylation was observed in the cells expressing wild-type HDAC3 (HDAC3(WT)), but not in cells overexpressing phosphorylation-defective HDAC3 (HDAC3(Y328/331A)). Phosphorylated HDAC3 showed relatively higher deacetylase activity, and PP2, which is a c-Src inhibitor, blocked HDAC3 phosphorylation and reduced its enzymatic activity. EGF treatment resulted in HDAC3 phosphorylation in both MDA-MB-231 and EGFR-overexpressing MCF7 (MCF7-EGFR) cells, but not in MCF7 cells. Total internal reflection fluorescence analysis showed that HDAC3 was recruited to the plasma membrane following EGF stimulation. HDAC3 inhibition with either c-Src knockdown or PP2 treatment significantly ameliorated the invasiveness of breast cancer cells. Altogether, our findings reveal an EGF signaling cascade involving EGFR, c-Src, and HDAC3 in breast cancer cells.-
dc.description.statementOfResponsibilityopen-
dc.languageEnglish-
dc.publisherMDPI-
dc.relation.isPartOfCELLS(Cells)-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.subject.MESHBreast Neoplasms / metabolism*-
dc.subject.MESHErbB Receptors / physiology-
dc.subject.MESHHEK293 Cells-
dc.subject.MESHHeLa Cells-
dc.subject.MESHHistone Deacetylases / physiology*-
dc.subject.MESHHumans-
dc.subject.MESHMCF-7 Cells-
dc.subject.MESHProto-Oncogene Mas-
dc.subject.MESHProto-Oncogene Proteins pp60(c-src) / physiology*-
dc.subject.MESHSignal Transduction-
dc.titleEGFR-c-Src-Mediated HDAC3 Phosphorylation Exacerbates Invasion of Breast Cancer Cells-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Biochemistry and Molecular Biology (생화학-분자생물학교실)-
dc.contributor.googleauthorSung-Min Kwak-
dc.contributor.googleauthorJaesung Seo-
dc.contributor.googleauthorJin-Taek Hwang-
dc.contributor.googleauthorGi-Jun Sung-
dc.contributor.googleauthorJi-Hye Song-
dc.contributor.googleauthorJi-Hoon Jeong-
dc.contributor.googleauthorSeung-Hyun Lee-
dc.contributor.googleauthorHo-Geun Yoon-
dc.contributor.googleauthorHyo-Kyoung Choi-
dc.contributor.googleauthorKyung-Chul Choi-
dc.identifier.doi10.3390/cells8080930-
dc.contributor.localIdA02625-
dc.contributor.localIdA02932-
dc.relation.journalcodeJ03774-
dc.identifier.pmid31430896-
dc.subject.keywordbreast cancer-
dc.subject.keywordc-Src-
dc.subject.keywordEGFR-
dc.subject.keywordHDAC3-
dc.subject.keywordpY-HDAC3Y328-
dc.subject.keyword331 antibody-
dc.contributor.alternativeNameYoon, Ho Geun-
dc.contributor.affiliatedAuthor윤호근-
dc.contributor.affiliatedAuthor이승현-
dc.citation.volume8-
dc.citation.number8-
dc.citation.startPage930-
dc.identifier.bibliographicCitationCELLS, Vol.8(8) : 930, 2019-08-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers

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