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- W2804673542 abstract "Poly (ADP-ribose)ylation is a dynamic protein modification that regulates multiple cellular processes. Here, we describe a system for identifying and characterizing PARylation events that exploits the ability of a PBZ (PAR-binding zinc finger) protein domain to bind PAR with high-affinity. By linking PBZ domains to bimolecular fluorescent complementation biosensors, we developed fluorescent PAR biosensors that allow the detection of temporal and spatial PARylation events in live cells. Exploiting transposon-mediated recombination, we integrate the PAR biosensor en masse into thousands of protein coding genes in living cells. Using these PAR-biosensor tagged cells in a genetic screen we carry out a large-scale identification of PARylation targets. This identifies CTIF (CBP80/CBP20-dependent translation initiation factor) as a novel PARylation target of the tankyrase enzymes in the centrosomal region of cells, which plays a role in the distribution of the centrosomal satellites." @default.
- W2804673542 created "2018-06-01" @default.
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- W2804673542 date "2018-05-22" @default.
- W2804673542 modified "2023-10-16" @default.
- W2804673542 title "Coupling bimolecular PARylation biosensors with genetic screens to identify PARylation targets" @default.
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- W2804673542 doi "https://doi.org/10.1038/s41467-018-04466-4" @default.
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