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.
Highlights
Post-translational modifications (PTMs) are an issue because they govern many biological processes during the development and disease by modifying the end products of expression
Arrest defective 1 (ARD1) is closely related to the cell cycle, Vo et al traced the cellular location of ARD1 during the cell cycle and observed that ARD1 is colocalized with Aurora kinase A (AuA) in the centrosome during cell division[68]
It is widely known that protein acetylation plays a pivotal role in regulating gene transcription by modulating histone acetylation and physiological and metabolic processes by mediating the acetylation of either chromatin or non-chromatin proteins in various cell compartments from the nucleus to the membrane
Summary
Tam Thuy Lu Vo1, Chul-Ho Jeong[1], Sooyeun Lee[1], Kyu-Won Kim[2], Eunyoung Ha3 and Ji Hae Seo[3]
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