TY - JOUR
T1 - In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation
AU - Aguilera-Gomez, Angelica
AU - van Oorschot, Marinke M.
AU - Veenendaal, Tineke
AU - Rabouille, Catherine
PY - 2016/11/22
Y1 - 2016/11/22
N2 - PARP catalysed ADP-ribosylation is a post-translational modification involved in several physiological and pathological processes, including cellular stress. In order to visualise both Poly-, and Mono-, ADP-ribosylation in vivo, we engineered specific fluorescent probes. Using them, we show that amino-acid starvation triggers an unprecedented display of mono-ADP-ribosylation that governs the formation of Sec body, a recently identified stress assembly that forms in Drosophila cells. We show that dPARP16 catalytic activity is necessary and sufficient for both amino-acid starvation induced mono-ADP-ribosylation and subsequent Sec body formation and cell survival. Importantly, dPARP16 catalyses the modification of Sec16, a key Sec body component, and we show that it is a critical event for the formation of this stress assembly. Taken together our findings establish a novel example for the role of mono-ADP-ribosylation in the formation of stress assemblies, and link this modification to a metabolic stress.
AB - PARP catalysed ADP-ribosylation is a post-translational modification involved in several physiological and pathological processes, including cellular stress. In order to visualise both Poly-, and Mono-, ADP-ribosylation in vivo, we engineered specific fluorescent probes. Using them, we show that amino-acid starvation triggers an unprecedented display of mono-ADP-ribosylation that governs the formation of Sec body, a recently identified stress assembly that forms in Drosophila cells. We show that dPARP16 catalytic activity is necessary and sufficient for both amino-acid starvation induced mono-ADP-ribosylation and subsequent Sec body formation and cell survival. Importantly, dPARP16 catalyses the modification of Sec16, a key Sec body component, and we show that it is a critical event for the formation of this stress assembly. Taken together our findings establish a novel example for the role of mono-ADP-ribosylation in the formation of stress assemblies, and link this modification to a metabolic stress.
UR - http://www.scopus.com/inward/record.url?scp=85000916621&partnerID=8YFLogxK
U2 - 10.7554/eLife.21475
DO - 10.7554/eLife.21475
M3 - Article
C2 - 27874829
AN - SCOPUS:85000916621
SN - 2050-084X
VL - 5
JO - eLife
JF - eLife
M1 - e21475
ER -