期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 404, 期 1, 页码 68-73出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.11.064
关键词
EGFR; CBP; Acetylation; Phosphorylation; SAHA
资金
- NIH [CA1109311, CA099031, CA126832, 1UL1RR024148]
- Breast Cancer SPORE [CA116199, CCSG CA16672]
- Patel Memorial Breast Cancer Research Fund
- MD Anderson Cancer Center-China Medical University
- Kadoorie Charitable Foundations
- [NSC97-3111-B-039]
- [NSC98-3111-B-039]
- [NHRI-EX98-9603BC]
- [DOH97-TD-I-111-TM003]
- [DOH 98-TD-I-111-TM002]
- [DOH97-TD-G-111-027]
- [DOH99-TD-C-111-005]
- [NSC99-2632-B-039-001-MY3]
Alteration of epidermal growth factor receptor (EGFR) is involved in various human cancers and has been intensively investigated. A plethora of evidence demonstrates that posttranslational modifications of EGFR play a pivotal role in controlling its function and metabolism. Here, we show that EGFR can be acetylated by CREB binding protein (CBP) acetyltransferase. Interestingly, EGFR acetylation affects its tyrosine phosphorylation, which may contribute to cancer cell resistance to histone deacetylase inhibitors (HDACIs). Since there is an increasing interest in using HDACIs to treat various cancers in the clinic, our current study provides insights and rationale for selecting effective therapeutic regimen. Consistent with the previous reports, we also show that HDACI combined with EGFR inhibitors achieves better therapeutic outcomes and provides a molecular rationale for the enhanced effect of combination therapy. Our results unveil a critical role of EGFR acetylation that regulates EGFR function, which may have an important clinical implication. Published by Elsevier Inc.
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