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KMID : 0620920180500070086
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Experimental & Molecular Medicine
2018 Volume.50 No. 7 p.86 ~ p.86
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Versatility of ARD1/NAA10-mediated protein lysine acetylation
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Vo Tam Thuy Lu
Jeong Chul-Ho
Lee Soo-Yeun
Kim Kyu-Won
Ha Eun-Young
Seo Ji-Hae
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Abstract
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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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KEYWORD
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Protein folding
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