Targeted large‐scale analysis of protein acetylation

Protein modifications are biologically important events that may be studied by mass spectrometry‐based high‐throughput proteome analyses. In recent years, several new technologies have emerged that have widened and deepened the targeted analysis of one important, albeit functionally ill‐defined modification, namely protein acetylation. This modification can take place both co‐ and post‐translationally by the transfer of acetyl groups under the catalysis of acetyltransferases. The acetyl group can modify either the α‐amino group at the N‐terminus, so‐called N‐terminal acetylation, or the ε‐amino group on the side chain of lysine residues. Here, we review several emerging targeted technologies to chart both N‐terminal acetylation as well as acetylation at the lysine side chain, on a proteome‐wide scale, highlighting in particular studies that have expanded the biological knowledge on the appearance and function of these common but functionally still less investigated co‐ and post‐translational modifications.