Reversible lysine acetylation regulates activity of human glycine N-acyltransferase-like 2 (hGLYATL2): implications for production of glycine-conjugated signaling molecules

• Published in: The Journal of biological chemistry Vol. 287; no. 20; pp. 16158 - 16167
• Main Authors: Waluk, Dominik P, Sucharski, Filip, Sipos, Laszlo, Silberring, Jerzy, Hunt, Mary C
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 11.05.2012
• Subjects: Acetylation; Acyltransferases - genetics; Acyltransferases - metabolism; Amino Acid Substitution; Animals; Arachidonic Acids - biosynthesis; Arachidonic Acids - genetics; Biochemistry; biokemi; Cell Biology; cellbiologi; Glycine - analogs & derivatives; Glycine - biosynthesis; Glycine - genetics; HEK293 Cells; HeLa Cells; Humans; Lipids; Mice; Molecular Biology; molekylärbiologi; Mutation, Missense; Oleic Acids - biosynthesis; Oleic Acids - genetics; Protein Processing, Post-Translational - physiology

Lysine acetylation is a major post-translational modification of proteins and regulates many physiological processes such as metabolism, cell migration, aging, and inflammation. Proteomic studies have identified numerous lysine-acetylated proteins in human and mouse models (Kim, S. C., Sprung, R., C...