Regulation of HDAC1 by Epidermal Growth Factor Receptor

Histone deacetylases (HDACs) are enzymes that catalyze the removal of acetylation from lysine residues of their substrates, the effect of which is to regulate a range of cellular processes, including gene transcription, cell cycle regulation, migration, and DNA damage repair, among others. Accordingly, the dysregulation of HDACs can contribute to the development of different diseases, such as immunological and metabolic disorders, as well as cancers. It is therefore critical to understand the mechanisms by which individual HDACs can be regulated and the conditions under which they occur. This study is an investigation of the regulation of histone deacetylase 1 (HDAC1) by tyrosine (Tyr) phosphorylation. We propose that HDAC1 may be phosphorylated at Tyr72 by epidermal growth factor receptor (EGFR) to the effect of promoting its anti-apoptosis function in lung adenocarcinoma cells. Given that HDAC1 and EGFR are both involved in promoting cancer growth and survival, this study identifies a new mechanism by which HDAC1 may be regulated such that it may be targeted to treat cancers with higher EGFR activity.

Author

• Bahl, Sonali

Language

• en

Keyword

• epigenetics
• tyrosine phosphorylation
• histone deacetylases
• lung adenocarcinoma
• epidermal growth factor receptor

Date created

• 2021

Type of Work

• Dissertation

License

• All rights reserved

Rights statement

• In Copyright

GW Unit

• Molecular Medicine

Degree

• Ph.D.

Advisor

• Seto, Edward

Committee Member(s)

• Fernandes, Rohan
• Caldovic, Ljubica
• Lee, Norman
• Chung, Inhee
• Chiappinelli, Katherine
• Hu, Yanfen

Persistent URL

•  https://scholarspace.library.gwu.edu/etd/gx41mj654