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PARP Proteins, Signal Transduction Mechanisms and Chromatin Remodeling
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PARP Proteins, Signal Transduction Mechanisms and Chromatin Remodeling

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Signaling".

Deadline for manuscript submissions: closed (10 May 2022) | Viewed by 9035

Special Issue Editor

Prof. Dr. Malka Cohen-Armon

E-Mail Website
Guest Editor
Sackler Faculty of Medicine, and Sagol School of Neuroscience, Tel-Aviv University, Tel-Aviv 69978, Israel
Interests: signal transduction mechanisms; voltage-dependent activation of G-proteins coupled receptors; ERK-PARP1 synergism; immediate-early gene expression in healthy and cancer cells; the implication of chromatin remodeling in long-term memory formation; PARP proteins in signal transduction mechanisms mediating mitosis

Special Issue Information

Dear Colleagues,

Activated PARP proteins catalyze the post-translational modification of proteins by adding negatively charged ADP-ribose moieties (polyADP-ribosylation). This modification of a variety of nuclear proteins, including PARP proteins, histones, high mobility group proteins, topoisomerases, gyrases, DNA methyltransferase and demethylases, and the insulator protein CTCF, causes chromatin remodeling. Thus, the epigenetic effect of polyADP-ribosylation has been recently disclosed.

PARP1, the most abundant nuclear PARP protein, is activated by binding to DNA breaks, and its polyADP-ribosylation plays a major role in DNA repair. Recently, the activation of PARP proteins, including PARP1, by a variety of signal transduction mechanisms has been disclosed in a variety of cell types and in response to various types of extracellular stimulation under physiological and pathological conditions. In addition, the binding and recruitment of ADP-ribose polymers to macrodomains in proteins is implicated in the recognition, interpretation and turnover of ADP-ribose signaling.

This Special Issue aims to contribute to the current knowledge on the implication of signal-induced polyADP-ribosylation of PARP proteins and their substrates and discuss their emerging potential as therapeutic targets.

Prof. Malka Cohen-Armon
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • PARP proteins in signal transduction mechanisms
  • macrodomain-containing proteins
  • PARP-mediated epigenetic effects

Published Papers (3 papers)

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Research

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17 pages, 1840 KiB  
Article
PARP1′s Involvement in RNA Polymerase II Elongation: Pausing and Releasing Regulation through the Integrator and Super Elongation Complex
by Elena A. Matveeva, Hejer Dhahri and Yvonne Fondufe-Mittendorf
Cells 2022, 11(20), 3202; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11203202 - 12 Oct 2022
Cited by 4 | Viewed by 1873
Abstract
RNA polymerase elongation along the gene body is tightly regulated to ensure proper transcription and alternative splicing events. Understanding the mechanism and factors critical in regulating the rate of RNA polymerase II elongation and processivity is clearly important. Recently we showed that PARP1, [...] Read more.
RNA polymerase elongation along the gene body is tightly regulated to ensure proper transcription and alternative splicing events. Understanding the mechanism and factors critical in regulating the rate of RNA polymerase II elongation and processivity is clearly important. Recently we showed that PARP1, a well-known DNA repair protein, when bound to chromatin, regulates RNA polymerase II elongation. However, the mechanism by which it does so is not known. In the current study, we aimed to tease out how PARP1 regulates RNAPII elongation. We show, both in vivo and in vitro, that PARP1 binds directly to the Integrator subunit 3 (IntS3), a member of the elongation Integrator complex. The association between the two proteins is mediated via the C-terminal domain of PARP1 to the C-terminal domain of IntS3. Interestingly, the occupancy of IntS3 along two PARP1 target genes mimicked that of PARP1, suggesting a role in its recruitment/assembly of elongation factors. Indeed, the knockdown of PARP1 resulted in differential chromatin association and gene occupancy of IntS3 and other key elongation factors. Most of these PARP1-mediated effects were due to the physical presence of PARP1 rather than its PARylation activity. These studies argue that PARP1 controls the progressive RNAPII elongation complexes. In summary, we present a platform to begin to decipher PARP1′s role in recruiting/scaffolding elongation factors along the gene body regions during RNA polymerase II elongation and gene regulation. Full article
(This article belongs to the Special Issue PARP Proteins, Signal Transduction Mechanisms and Chromatin Remodeling)
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16 pages, 2895 KiB  
Article
Temporal and Site-Specific ADP-Ribosylation Dynamics upon Different Genotoxic Stresses
by Sara C. Buch-Larsen, Alexandra K. L. F. S. Rebak, Ivo A. Hendriks and Michael L. Nielsen
Cells 2021, 10(11), 2927; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10112927 - 28 Oct 2021
Cited by 11 | Viewed by 2544
Abstract
The DNA damage response revolves around transmission of information via post-translational modifications, including reversible protein ADP-ribosylation. Here, we applied a mass-spectrometry-based Af1521 enrichment technology for the identification and quantification of ADP-ribosylation sites as a function of various DNA damage stimuli and time. In [...] Read more.
The DNA damage response revolves around transmission of information via post-translational modifications, including reversible protein ADP-ribosylation. Here, we applied a mass-spectrometry-based Af1521 enrichment technology for the identification and quantification of ADP-ribosylation sites as a function of various DNA damage stimuli and time. In total, we detected 1681 ADP-ribosylation sites residing on 716 proteins in U2OS cells and determined their temporal dynamics after exposure to the genotoxins H2O2 and MMS. Intriguingly, we observed a widespread but low-abundance serine ADP-ribosylation response at the earliest time point, with later time points centered on increased modification of the same sites. This suggests that early serine ADP-ribosylation events may serve as a platform for an integrated signal response. While treatment with H2O2 and MMS induced homogenous ADP-ribosylation responses, we observed temporal differences in the ADP-ribosylation site abundances. Exposure to MMS-induced alkylating stress induced the strongest ADP-ribosylome response after 30 min, prominently modifying proteins involved in RNA processing, whereas in response to H2O2-induced oxidative stress ADP-ribosylation peaked after 60 min, mainly modifying proteins involved in DNA damage pathways. Collectively, the dynamic ADP-ribosylome presented here provides a valuable insight into the temporal cellular regulation of ADP-ribosylation in response to DNA damage. Full article
(This article belongs to the Special Issue PARP Proteins, Signal Transduction Mechanisms and Chromatin Remodeling)
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Review

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13 pages, 1998 KiB  
Review
A Long-Lasting PARP1-Activation Mediates Signal-Induced Gene Expression
by Malka Cohen-Armon
Cells 2022, 11(9), 1576; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11091576 - 07 May 2022
Cited by 3 | Viewed by 3601
Abstract
This overview presents recent evidence for a long-lasting PARP1 activation by a variety of signal transduction mechanisms, mediating signal-induced gene expression and chromatin remodeling. This mode of PARP1 activation has been reported in a variety of cell types, under physiological conditions. In this [...] Read more.
This overview presents recent evidence for a long-lasting PARP1 activation by a variety of signal transduction mechanisms, mediating signal-induced gene expression and chromatin remodeling. This mode of PARP1 activation has been reported in a variety of cell types, under physiological conditions. In this mechanism, PARP1 is not transiently activated by binding to DNA breaks. Moreover, damaged DNA interfered with this long-lasting PARP1 activation. Full article
(This article belongs to the Special Issue PARP Proteins, Signal Transduction Mechanisms and Chromatin Remodeling)
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