ADPriboDB: The database of ADP-ribosylated proteins

Vivelo, Christina A.; Wat, Ricky; Agrawal, Charul; Tee, Hui Yi; Leung, Anthony K.L.

doi:10.1093/nar/gkx035

Cited by 5 publications

(3 citation statements)

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“…Because PARP1 was identified in the DTX2 interactome and PARylation is a common posttranslational feature of many identified binding partners of DTX2 including SPT16 and histone H3.1 as well as DTX2 itself ( 21 , 24 ), we next investigated the effects of ABT-888 (veliparib), a PARP1 and PARP2 inhibitor, on substrate binding and ubiquitination. In the presence of ABT-888, none of the selected binding partners from the Myc-trap pull-down coimmunoprecipitated with DTX2 ( Fig.…”

Section: Resultsmentioning

confidence: 99%

DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination

et al. 2020

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Cross-talk between ubiquitination and ADP-ribosylation regulates spatiotemporal recruitment of key players in many signaling pathways. The DELTEX family ubiquitin ligases (DTX1 to DTX4 and DTX3L) are characterized by a RING domain followed by a C-terminal domain (DTC) of hitherto unknown function. Here, we use two label-free mass spectrometry techniques to investigate the interactome and ubiquitinated substrates of human DTX2 and identify a large proportion of proteins associated with the DNA damage repair pathway. We show that DTX2-catalyzed ubiquitination of these interacting proteins requires PARP1/2-mediated ADP-ribosylation and depends on the DTC domain. Using a combination of structural, biochemical, and cell-based techniques, we show that the DTX2 DTC domain harbors an ADP-ribose–binding pocket and recruits poly-ADP-ribose (PAR)–modified proteins for ubiquitination. This PAR-binding property of DTC domain is conserved across the DELTEX family E3s. These findings uncover a new ADP-ribose–binding domain that facilitates PAR-dependent ubiquitination.

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Section: Resultsmentioning

confidence: 99%

DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination

et al. 2020

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“…These PARPs are implicated in the regulation of numerous DNA repair pathways, and PARP activation on DNA damage sites appears to have a dual function, for example, local PAR synthesis for recruitment of repair enzymes and trans-PARylation of repair factors [ 3 , 6 , 7 , 8 , 9 ]. Although PARP1 has been found to be a major acceptor of PAR during its own activation [ 10 , 11 ], to date, approximately 2389 proteins have been identified as PARylation targets after different types of genotoxic stress [ 12 ]. Even though numerous PARP targets have been found, many of them can both be modified by PAR and/or directly interact with the PAR synthesised by PARPs [ 1 , 8 , 13 , 14 , 15 ].…”

Section: Introductionmentioning

confidence: 99%

Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1

et al. 2020

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Y-box-binding protein 1 (YB-1) is a multifunctional positively charged protein that interacts with DNA or RNA and poly(ADP-ribose) (PAR). YB-1 is poly(ADP-ribosyl)ated and stimulates poly(ADP-ribose) polymerase 1 (PARP1) activity. Here, we studied the mechanism of YB-1-dependent PAR synthesis by PARP1 in vitro using biochemical and atomic force microscopy assays. PAR synthesis activity of PARP1 is known to be facilitated by co-factors such as Mg2+. However, in contrast to an Mg2+-dependent reaction, the activation of PARP1 by YB-1 is accompanied by overall up-regulation of protein PARylation and shortening of the PAR polymer. Therefore, YB-1 and cation co-factors stimulated PAR synthesis in divergent ways. PARP1 autoPARylation in the presence of YB-1 as well as trans-PARylation of YB-1 are greatly affected by the type of damaged DNA, suggesting that PARP1 activation depends on the formation of a PARP1–YB-1–DNA ternary complex. An unstructured C-terminal part of YB-1 involved in an interaction with PAR behaves similarly to full-length YB-1, indicating that both DNA and PAR binding are involved in the stimulation of PARP1 activity by YB-1. Thus, YB-1 is likely linked to the regulation of PARylation events in cells via an interaction with PAR and damaged DNA.

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“…PARP2 has multiple PARylation targets including proteins involved in transcription, translation, mitochondrial organization, redox balance, DNA repair, PARylation machinery (e.g. HPF1) (Refs 53, 56, 94, 95, 96, 97, 98, 99). Nucleic acid structures may also be sites of ADP-ribosylation (Ref.…”

Section: Parp2 Structure and Enzymatic Activitymentioning

confidence: 99%

Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?

Szántó,

Yélamos,

Bai

2024

Expert Rev. Mol. Med.

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PARP2, that belongs to the family of ADP-ribosyl transferase enzymes (ART), is a discovery of the millennium, as it was identified in 1999. Although PARP2 was described initially as a DNA repair factor, it is now evident that PARP2 partakes in the regulation or execution of multiple biological processes as inflammation, carcinogenesis and cancer progression, metabolism or oxidative stress-related diseases. Hereby, we review the involvement of PARP2 in these processes with the aim of understanding which processes are specific for PARP2, but not for other members of the ART family. A better understanding of the specific functions of PARP2 in all of these biological processes is crucial for the development of new PARP-centred selective therapies.

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ADPriboDB: The database of ADP-ribosylated proteins

Cited by 5 publications

References 0 publications

DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination

DELTEX2 C-terminal domain recognizes and recruits ADP-ribosylated proteins for ubiquitination

Regulation of Poly(ADP-Ribose) Polymerase 1 Activity by Y-Box-Binding Protein 1

Specific and shared biological functions of PARP2 – is PARP2 really a lil’ brother of PARP1?

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