Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites

Rosenthal, Florian

doi:10.2741/4266

Cited by 25 publications

(29 citation statements)

References 134 publications

(176 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Though the modification was discovered over 50 years ago (34,35), it was only until recently that several proteomics techniques have been developed to identify the ADP-ribosylation sites (9,36). Such site information will provide initial insights to generate hypotheses for testing the function of ADP-ribosylation in modified substrates.…”

Section: Introductionmentioning

confidence: 99%

ADPriboDB: The database of ADP-ribosylated proteins

et al. 2016

View full text Add to dashboard Cite

ADP-ribosylation refers to the addition of one or more ADP-ribose units onto proteins post-translationally. This protein modification is often added by ADP-ribosyltransferases, commonly known as PARPs, but it can also be added by other enzymes, including sirtuins or bacterial toxins. While past literature has utilized a variety of methods to identify ADP-ribosylated proteins, recent proteomics studies bring the power of mass spectrometry to determine sites of the modification. To appreciate the diverse roles of ADP-ribosylation across the proteome, we have created ADPriboDB – a database of ADP-ribosylated proteins (http://ADPriboDB.leunglab.org). Each entry of ADPriboDB is annotated manually by at least two independent curators from the literature between January 1975 and July 2015. The current database includes over 12 400 protein entries from 459 publications, identifying 2389 unique proteins. Here, we describe the structure and the current state of ADPriboDB as well as the criteria for entry inclusion. Using this aggregate data, we identified a statistically significant enrichment of ADP-ribosylated proteins in non-membranous RNA granules. To our knowledge, ADPriboDB is the first publicly available database encapsulating ADP-ribosylated proteins identified from the past 40 years, with a hope to facilitate the research of both basic scientists and clinicians to better understand ADP-ribosylation at the molecular level.

show abstract

Section: Introductionmentioning

confidence: 99%

ADPriboDB: The database of ADP-ribosylated proteins

et al. 2016

View full text Add to dashboard Cite

show abstract

“…lysine, which usually contributes to direct contact with DNA (28). Along with the aspartic and glutamic acid residues, lysine residues are considered as main ADP-ribose acceptor sites (14,29,30).…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP-ribose) Polymerase 1 Modulates Interaction of the Nucleotide Excision Repair Factor XPC-RAD23B with DNA via Poly(ADP-ribosyl)ation

Maltseva

Rechkunova

Sukhanova

et al. 2015

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Poly(ADP-ribosyl)ation of DNA repair proteins is essential for the regulation of DNA repair processes. Results: Both subunits of the nucleotide excision repair factor XPC-RAD23B are poly(ADP-ribosyl)ated by PARP1. Conclusion: PARP1 influences the interaction of XPC-RAD23B with DNA via PAR synthesis. Significance: This study provides direct evidence for XPC-RAD23B belonging to the targets of poly(ADP-ribosyl)ation catalyzed by PARP1.

show abstract

“…ARTD1 possesses an intrinsic enzymatic activity that catalyzes the transfer of ADP-ribose (ADPr) units from NAD (NAD ϩ ) onto target gene regulatory proteins, thereby modulating their activities, functions, and interacting partners (32,33).…”

mentioning

confidence: 99%

ARTD1 Suppresses Interleukin 6 Expression by Repressing MLL1-Dependent Histone H3 Trimethylation

Minotti

Andersson

Hottiger

2015

Molecular and Cellular Biology

View full text Add to dashboard Cite

b ADP-ribosyltransferase diphtheria-toxin like 1/poly(ADP-ribose) polymerase 1 (ARTD1/PARP1) is a chromatin-associated protein in the nucleus and plays an important role in different cellular processes such as regulation of gene transcription. ARTD1 has been shown to coregulate the inflammatory response by modulating the activity of the transcription factor nuclear factor B (NF-B), the principal regulator of interleukin 6 (IL-6), an important inflammatory cytokine implicated in a variety of diseases such as cancer. However, to what extent and how ARTD1 regulates IL-6 transcription has not been clear. Here, we show that ARTD1 suppresses lipopolysaccharide (LPS)-induced IL-6 expression in macrophages, without affecting the recruitment of the NF-B subunit RelA to the IL-6 promoter and independent of its enzymatic activity. Interestingly, knockdown of ARTD1 did not alter H3 occupancy but increased LPS-induced trimethylation of histone 3 at lysine 4 (H3K4me3), a hallmark of transcriptionally active genes. We found that ARTD1 mediates its effect through the methyltransferase MLL1, by catalyzing H3K4me3 at the IL-6 promoter and forming a complex with NF-B. These results demonstrate that ARTD1 modulates IL-6 expression by regulating the function of an NF-B enhanceosome complex, which involves MLL1 and does not require ADP-ribosylation.

show abstract

Identification of ADP-ribosylated peptides and ADP-ribose acceptor sites

Cited by 25 publications

References 134 publications

ADPriboDB: The database of ADP-ribosylated proteins

ADPriboDB: The database of ADP-ribosylated proteins

Poly(ADP-ribose) Polymerase 1 Modulates Interaction of the Nucleotide Excision Repair Factor XPC-RAD23B with DNA via Poly(ADP-ribosyl)ation

ARTD1 Suppresses Interleukin 6 Expression by Repressing MLL1-Dependent Histone H3 Trimethylation

Contact Info

Product

Resources

About