TY - CHAP
T1 - Protein Lysine Acylation: Abundance, Dynamics and Function
AU - Pougovkina, Olga
AU - de Boer, Vincent
PY - 2016/11/18
Y1 - 2016/11/18
N2 - Lysine acylation comprises a group of post-translational modifications which involve the transfer of an acyl group to ε-amino group of a lysine residue. Most studied acylation modification is acetylation, however recently, a number of new acylation modifications have been discovered. These include formylation, propionylation, butyrylation, malonylation, succinylation, glutarylation and crotonylation. In this chapter, we review the discovery of various acylation modifications and the current insight into their function, regulation and dynamics.
AB - Lysine acylation comprises a group of post-translational modifications which involve the transfer of an acyl group to ε-amino group of a lysine residue. Most studied acylation modification is acetylation, however recently, a number of new acylation modifications have been discovered. These include formylation, propionylation, butyrylation, malonylation, succinylation, glutarylation and crotonylation. In this chapter, we review the discovery of various acylation modifications and the current insight into their function, regulation and dynamics.
U2 - 10.1007/978-94-024-0962-8_3
DO - 10.1007/978-94-024-0962-8_3
M3 - Chapter
SN - 9789402409611
T3 - Proteins and Cell Regulation
SP - 41
EP - 69
BT - Sirtuins
A2 - Houtkooper, Riekelt H.
PB - Springer
CY - Dordrecht
ER -