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• W2551954408 abstract "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." @default.
• W2551954408 created "2016-11-30" @default.
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• W2551954408 date "2016-11-22" @default.
• W2551954408 modified "2023-10-09" @default.
• W2551954408 title "In vivo vizualisation of mono-ADP-ribosylation by dPARP16 upon amino-acid starvation" @default.
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• W2551954408 doi "https://doi.org/10.7554/elife.21475" @default.
• W2551954408 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5127640" @default.
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