0 395

Cited 1 times in

Tyrosine phosphorylation of HDAC3 by Src kinase mediates proliferation of HER2-positive breast cancer cells

DC Field Value Language
dc.contributor.author김미정-
dc.contributor.author윤호근-
dc.contributor.author윤호근-
dc.date.accessioned2019-03-15T02:26:19Z-
dc.date.available2019-03-15T02:26:19Z-
dc.date.issued2019-
dc.identifier.issn0021-9541-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/167480-
dc.description.abstractThe role of histone deacetylase 3 (HDAC3) is to repress the expression of various genes by eliminating acetyl group from histone. Thus, the regulation of HDAC3 activity is essential to maintain cellular homeostasis. In this study, we found that HDAC3 interacts with c-Src kinase. However, the interaction between HDAC3 and c-Src was previously reported, it has still been ambiguous whether c-Src phosphorylates HDAC3 and affects the function of HDAC3. First, we confirmed that HDAC3 directly binds to c-Src, and c-Src identified to interact with C-terminal domain (277-428 a.a.) of HDAC3. c-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form). When these tyrosine residues are all substituted for alanine residues, the deacetylase activity of mutant HDAC3 was abolished. In addition, a proliferation of HER2-positive breast cancer cells expressing phosphorylation deficient mutant HDAC3 is decreased in comparison with control cells. Thus, our findings suggested that phosphorylation of HDAC3 by c-Src kinase regulates the HDAC3 activity and the proliferation of breast cancer cells.-
dc.description.statementOfResponsibilityrestriction-
dc.languageEnglish-
dc.publisherWiley-Liss-
dc.relation.isPartOfJOURNAL OF CELLULAR PHYSIOLOGY-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.titleTyrosine phosphorylation of HDAC3 by Src kinase mediates proliferation of HER2-positive breast cancer cells-
dc.typeArticle-
dc.contributor.collegeCollege of Medicine (의과대학)-
dc.contributor.departmentDept. of Biochemistry and Molecular Biology (생화학-분자생물학교실)-
dc.contributor.googleauthorJaesung Seo-
dc.contributor.googleauthorGaram Guk-
dc.contributor.googleauthorSeung‐Ho Park-
dc.contributor.googleauthorMi‐Hyeon Jeong-
dc.contributor.googleauthorJi‐Hoon Jeong-
dc.contributor.googleauthorHo‐Geun Yoon-
dc.contributor.googleauthorKyung‐Chul Choi-
dc.identifier.doi10.1002/jcp.27378-
dc.contributor.localIdA00450-
dc.contributor.localIdA02625-
dc.contributor.localIdA02625-
dc.contributor.localIdA02625-
dc.contributor.localIdA02625-
dc.relation.journalcodeJ01304-
dc.identifier.eissn1097-4652-
dc.identifier.pmid30317579-
dc.identifier.urlhttps://onlinelibrary.wiley.com/doi/full/10.1002/jcp.27378-
dc.subject.keywordHDAC3-
dc.subject.keywordbreast cancer-
dc.subject.keywordc-Src-
dc.subject.keywordproliferation-
dc.subject.keywordtyrosine phosphorylation-
dc.contributor.alternativeNameKim, Mi Jeong-
dc.contributor.affiliatedAuthor김미정-
dc.contributor.affiliatedAuthor윤호근-
dc.contributor.affiliatedAuthor윤호근-
dc.contributor.affiliatedAuthor윤호근-
dc.contributor.affiliatedAuthor윤호근-
dc.citation.volume234-
dc.citation.number5-
dc.citation.startPage6428-
dc.citation.endPage6436-
dc.identifier.bibliographicCitationJOURNAL OF CELLULAR PHYSIOLOGY, Vol.234(5) : 6428-6436, 2019-
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.