Versatility of ARD1/NAA10-mediated protein lysine acetylation
- Author(s)
- Tam Thuy Lu Vo; Chul-Ho Jeong; Sooyeun Lee; Kyu-Won Kim; Eunyoung Ha; Ji Hae Seo
- Keimyung Author(s)
- Jung, Chul Ho; Ha, Eun Young; Seo, Ji Hye
- Department
- Dept. of Psychiatry (정신건강의학)
Dept. of Biochemistry (생화학)
- Journal Title
- Experimental & Molecular Medicine
- Issued Date
- 2018
- Volume
- 50
- Issue
- 7
- Abstract
- Post-translational modifications (PTMs) are chemical alterations that occur in proteins that play critical roles in various cellular functions. Lysine acetylation is an important PTM in eukaryotes, and it is catalyzed by lysine acetyltransferases (KATs). KATs transfer acetyl-coenzyme A to the internal lysine residue of substrate proteins. Arrest defective 1 (ARD1) is a member of the KAT family. Since the identification of its KAT activity 15 years ago, many studies have revealed that diverse cellular proteins are acetylated by ARD1. ARD1-mediated lysine acetylation is a key switch that regulates the enzymatic activities and biological functions of proteins and influences cell biology from development to pathology. In this review, we summarize protein lysine acetylation mediated by ARD1 and describe the biological meanings of this modification.
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