Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG

• Published in: Nature communications Vol. 15; no. 1; p. 4239
• Main Authors: Longarini, Edoardo José, Matić, Ivan
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 18.05.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 13; 13/1; 14; 14/63; 631/45/173; 631/45/475; 631/92/458/2389; 82/29; 82/58; 96; 96/35; Adenosine diphosphate; ADP; ADP-Ribosylation; Antibodies; Aspartic Acid - metabolism; Damage; Deoxyribonucleic acid; DNA; DNA Damage; Esters - chemistry; Esters - metabolism; Glutamic Acid - metabolism; Glycoside Hydrolases - metabolism; HEK293 Cells; Humanities and Social Sciences; Humans; Lability; Mass spectrometry; Mass spectroscopy; multidisciplinary; Poly (ADP-Ribose) Polymerase-1 - metabolism; Poly(ADP-ribose) polymerase; Post-translation; Protein Processing, Post-Translational; Ribose; Science; Science (multidisciplinary); Serine; Signal Transduction; Threonine; Ubiquitination

Ester-linked post-translational modifications, including serine and threonine ubiquitination, have gained recognition as important cellular signals. However, their detection remains a significant challenge due to the chemical lability of the ester bond. This is the case even for long-known modificat...