In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation

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.

KW - ter sites poly(adp-ribose) proteins drosophila binding sec16 differentiation identification macrodomains regulator Life Sciences & Biomedicine - Other Topics

U2 - 10.7554/eLife.21475

DO - 10.7554/eLife.21475

M3 - Article

C2 - 27874829

SN - 2050-084X

VL - 5

SP - 23

JO - eLife

JF - eLife

ER -