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

Authors
 Jaesung Seo  ;  Garam Guk  ;  Seung‐Ho Park  ;  Mi‐Hyeon Jeong  ;  Ji‐Hoon Jeong  ;  Ho‐Geun Yoon  ;  Kyung‐Chul Choi 
Citation
 JOURNAL OF CELLULAR PHYSIOLOGY, Vol.234(5) : 6428-6436, 2019 
Journal Title
 JOURNAL OF CELLULAR PHYSIOLOGY 
ISSN
 0021-9541 
Issue Date
2019
Keywords
HDAC3 ; breast cancer ; c-Src ; proliferation ; tyrosine phosphorylation
Abstract
The 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.
Full Text
https://onlinelibrary.wiley.com/doi/full/10.1002/jcp.27378
DOI
10.1002/jcp.27378
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Mi Jeong(김미정) ORCID logo https://orcid.org/0000-0002-0758-7145
Yoon, Ho Geun(윤호근) ORCID logo https://orcid.org/0000-0003-2718-3372
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/167480
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