Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz +11 more
wiley +1 more source
Proteasome Regulation by ADP-Ribosylation [PDF]
Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and survival. Defects in this process are associated with diseases such as cancer and neurodegenerative disorders. The 26S proteasome is a large protease complex that degrades ubiquitinated proteins. Here, we show that ADP-ribosylation promotes 26S proteasome activity
Cho-Park, Park F., Steller, Hermann
openaire +2 more sources
The Viral Macrodomain Counters Host Antiviral ADP-Ribosylation
Macrodomains, enzymes that remove ADP-ribose from proteins, are encoded by several families of RNA viruses and have recently been shown to counter innate immune responses to virus infection.
Yousef M. O. Alhammad, Anthony R. Fehr
semanticscholar +1 more source
Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin [PDF]
A critical step of DNA single-strand break repair is the rapid recruitment of the scaffold protein XRCC1 that interacts with, stabilizes and stimulates multiple enzymatic components of the repair process. XRCC1 recruitment is promoted by PARP1, an enzyme
Abdou +7 more
core +1 more source
Plecstatin inhibits hepatocellular carcinoma tumorigenesis and invasion through cytolinker plectin
The ruthenium‐based metallodrug plecstatin exerts its anticancer effect in hepatocellular carcinoma (HCC) primarily through selective targeting of plectin. By disrupting plectin‐mediated cytoskeletal organization, plecstatin inhibits anchorage‐dependent growth, cell polarization, and tumor cell dissemination.
Zuzana Outla +10 more
wiley +1 more source
Interplay of Histone Marks with Serine ADP-Ribosylation
Summary: Serine ADP-ribosylation (Ser-ADPr) is a recently discovered protein modification that is catalyzed by PARP1 and PARP2 when in complex with the eponymous histone PARylation factor 1 (HPF1).
Edward Bartlett +6 more
doaj +1 more source
The impact of PARPs and ADP-ribosylation on inflammation and host–pathogen interactions
In this review, Fehr et al. summarize the current understanding of the mechanisms by which PARPs promote or suppress proinflammatory activation of macrophages, and also discuss various other roles PARPs play in virus infections.
Anthony R. Fehr +5 more
semanticscholar +1 more source
Serine ADP-ribosylation in DNA-damage response regulation.
PARP1 and PARP2 govern the DNA-damage response by catalysing the reversible post-translational modification ADP-ribosylation. During the repair of DNA lesions, PARP1 and PARP2 combine with an accessory factor HPF1, which is required for the modification ...
L. Palazzo, M. Suskiewicz, I. Ahel
semanticscholar +1 more source
SIRT4 positively regulates autophagy via ULK1, but independently of HDAC6 and OPA1
Cells expressing SIRT4 (H161Y), a catalytically inactive mutant of the sirtuin SIRT4, fail to upregulate LC3B‐II and exhibit a reduced autophagic flux under stress conditions. Interestingly, SIRT4(H161Y) promotes phosphorylation of ULK1 at S638 and S758 that are associated with inhibition of autophagy initiation.
Isabell Lehmkuhl +13 more
wiley +1 more source
A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation. [PDF]
Nicotinamide adenine dinucleotide (NAD+)-dependent ADP-ribosylation plays important roles in physiology and pathophysiology. It has been challenging to study this key type of enzymatic post-translational modification in particular for protein poly-ADP ...
Chen, Jingwen +9 more
core +1 more source

