A Chemical Genetic Approach for Identifying Family-member Specific Targets of MonoPARPs
OHSU # 2162
Poly-(ADP-ribose) polymerases (PARPs) are emerging as critical regulators of cell function in both normal physiology and disease, particularly neurodegeneration and cancer. These enzymes transfer the ADP-ribose moiety from its substrate, nicotinamide adenine dinucleotide (NAD+), to amino acids of target proteins. Mono-PARPs, also known as mono-ADP-rybosyltransferases (mono-ARTDs), catalyze the transfer of a single unit of ADP-ribose from NAD+ to target proteins. The cellular functions of mono-ADP-ribosylation are not nearly as well understood as they are for poly-ADP-ribosylation, which is due in part to the lack of available chemical tools to study mono-PARPs. Researchers at Oregon Health & Science University have developed a strategy to identify direct protein targets of specific mono-PARPs. This novel method is expected to significantly advance our understanding of the cellular functions of mono-PARPs.
Cohen, Michael S. et. al. Engineering the substrate specificity of ADP-ribosyltransferases for identifying direct protein targets. J. Am. Chem. Soc. 2014; 136:5201-5204.
- Michael Cohen, SM.Physiology & Pharmacology
- Ian Carter-O'Connell, SM.Phys and Pharm
- Rory Morgan, SM.Phys and Pharm
- Haihong Jin, SM.Physiology & Pharmacology
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