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The Role of Post-translational Modifications in Chromatin and Cancer
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The Role of Post-translational Modifications in Chromatin and Cancer

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Oncology".

Deadline for manuscript submissions: closed (31 July 2022) | Viewed by 19795

Special Issue Editor

Dr. Emilio Lecona

E-Mail Website
Guest Editor
Centre for Molecular Biology Severo Ochoa (CBMSO)
Interests: DNA replication, replication stress, ubiquitin, SUMO, cancer, chromatin

Special Issue Information

Dear Colleagues,

The transmission, maintenance and expression of the genetic information in the cell is achieved through the processes of DNA replication, repair and transcription that converge on chromatin as a common substrate. Post-translational modifications (PTMs) of proteins in chromatin play a central role in the spatial and temporal co-ordination of chromatin metabolism allowing cells to express a specific transcriptional program while copying their DNA and ensuring the maintenance of genomic instability. These PTMs control the activity, stability and interaction of both histone and non-histone proteins being deposited and removed by several dedicated sets of enzymes. The dysregulation of these pathways can lead to cancer development by fostering uncontrolled proliferation or promoting the loss of cell identity. In addition, cell transformation can also elicit changes in the PTMs present on proteins on chromatin what can contribute to the acquisition of specific phenotypes by cancer cells. These enzymes are potential targets for cancer treatment and many advances have been made in the last years in the development of inhibitors that will specifically target PTMs altered in cancer cells through the inhibition of the enzymes that deposit or remove specific modifications.

For this special issue we look forward to receiving reviews or original works that delve deeper in the mechanisms through which PTMs control chromatin metabolism from replication to transcription and repair, how these processes contribute to the development of cancer and the recent advances in the development of therapies that target the enzymes in charge of the specific PTMs of proteins in chromatin.

Dr. Emilio Lecona
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • DNA Replication, Repair and Transcription
  • Post-translational modifications
  • Chromatin
  • Acetylation, methylation, phosphorylation
  • Ubiquitination and ubiquitin-like modifiers
  • Histone modifications
  • Chromatin
  • Cancer
  • Targeted cancer therapy
  • Epigenetics and cancer

Published Papers (4 papers)

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Review

14 pages, 824 KiB  
Review
DNA Damage Response Regulation by Histone Ubiquitination
by Miyu Sekiguchi and Nobuko Matsushita
Int. J. Mol. Sci. 2022, 23(15), 8187; https://doi.org/10.3390/ijms23158187 - 25 Jul 2022
Cited by 14 | Viewed by 3103
Abstract
Cells are constantly exposed to numerous genotoxic stresses that induce DNA damage. DNA double-strand breaks (DSBs) are among the most serious damages and should be systematically repaired to preserve genomic integrity. The efficiency of repair is closely associated with chromatin structure, which is [...] Read more.
Cells are constantly exposed to numerous genotoxic stresses that induce DNA damage. DNA double-strand breaks (DSBs) are among the most serious damages and should be systematically repaired to preserve genomic integrity. The efficiency of repair is closely associated with chromatin structure, which is regulated by posttranslational modifications of histones, including ubiquitination. Recent evidence shows crosstalk between histone ubiquitination and DNA damage responses, suggesting an integrated model for the systematic regulation of DNA repair. There are two major pathways for DSB repair, viz., nonhomologous end joining and homologous recombination, and the choice of the pathway is partially controlled by posttranslational modifications of histones, including ubiquitination. Histone ubiquitination changes chromatin structure in the vicinity of DSBs and serves as a platform to select and recruit repair proteins; the removal of these modifications by deubiquitinating enzymes suppresses the recruitment of repair proteins and promotes the convergence of repair reactions. This article provides a comprehensive overview of the DNA damage response regulated by histone ubiquitination in response to DSBs. Full article
(This article belongs to the Special Issue The Role of Post-translational Modifications in Chromatin and Cancer)
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23 pages, 2755 KiB  
Review
Insights in Post-Translational Modifications: Ubiquitin and SUMO
by Daniel Salas-Lloret and Román González-Prieto
Int. J. Mol. Sci. 2022, 23(6), 3281; https://doi.org/10.3390/ijms23063281 - 18 Mar 2022
Cited by 33 | Viewed by 6870
Abstract
Both ubiquitination and SUMOylation are dynamic post-translational modifications that regulate thousands of target proteins to control virtually every cellular process. Unfortunately, the detailed mechanisms of how all these cellular processes are regulated by both modifications remain unclear. Target proteins can be modified by [...] Read more.
Both ubiquitination and SUMOylation are dynamic post-translational modifications that regulate thousands of target proteins to control virtually every cellular process. Unfortunately, the detailed mechanisms of how all these cellular processes are regulated by both modifications remain unclear. Target proteins can be modified by one or several moieties, giving rise to polymers of different morphology. The conjugation cascades of both modifications comprise a few activating and conjugating enzymes but close to thousands of ligating enzymes (E3s) in the case of ubiquitination. As a result, these E3s give substrate specificity and can form polymers on a target protein. Polymers can be quickly modified forming branches or cleaving chains leading the target protein to its cellular fate. The recent development of mass spectrometry(MS) -based approaches has increased the understanding of ubiquitination and SUMOylation by finding essential modified targets in particular signaling pathways. Here, we perform a concise overview comprising from the basic mechanisms of both ubiquitination and SUMOylation to recent MS-based approaches aimed to find specific targets for particular E3 enzymes. Full article
(This article belongs to the Special Issue The Role of Post-translational Modifications in Chromatin and Cancer)
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31 pages, 1422 KiB  
Review
Histone Modifications and Their Targeting in Lymphoid Malignancies
by Miranda Fernández-Serrano, René Winkler, Juliana C. Santos, Marguerite-Marie Le Pannérer, Marcus Buschbeck and Gaël Roué
Int. J. Mol. Sci. 2022, 23(1), 253; https://doi.org/10.3390/ijms23010253 - 27 Dec 2021
Cited by 7 | Viewed by 5574
Abstract
In a wide range of lymphoid neoplasms, the process of malignant transformation is associated with somatic mutations in B cells that affect the epigenetic machinery. Consequential alterations in histone modifications contribute to disease-specific changes in the transcriptional program. Affected genes commonly play important [...] Read more.
In a wide range of lymphoid neoplasms, the process of malignant transformation is associated with somatic mutations in B cells that affect the epigenetic machinery. Consequential alterations in histone modifications contribute to disease-specific changes in the transcriptional program. Affected genes commonly play important roles in cell cycle regulation, apoptosis-inducing signal transduction, and DNA damage response, thus facilitating the emergence of malignant traits that impair immune surveillance and favor the emergence of different B-cell lymphoma subtypes. In the last two decades, the field has made a major effort to develop therapies that target these epigenetic alterations. In this review, we discuss which epigenetic alterations occur in B-cell non-Hodgkin lymphoma. Furthermore, we aim to present in a close to comprehensive manner the current state-of-the-art in the preclinical and clinical development of epigenetic drugs. We focus on therapeutic strategies interfering with histone methylation and acetylation as these are most advanced in being deployed from the bench-to-bedside and have the greatest potential to improve the prognosis of lymphoma patients. Full article
(This article belongs to the Special Issue The Role of Post-translational Modifications in Chromatin and Cancer)
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16 pages, 1738 KiB  
Review
Coordinating DNA Replication and Mitosis through Ubiquitin/SUMO and CDK1
by Antonio Galarreta, Pablo Valledor, Oscar Fernandez-Capetillo and Emilio Lecona
Int. J. Mol. Sci. 2021, 22(16), 8796; https://doi.org/10.3390/ijms22168796 - 16 Aug 2021
Cited by 5 | Viewed by 3566
Abstract
Post-translational modification of the DNA replication machinery by ubiquitin and SUMO plays key roles in the faithful duplication of the genetic information. Among other functions, ubiquitination and SUMOylation serve as signals for the extraction of factors from chromatin by the AAA ATPase VCP. [...] Read more.
Post-translational modification of the DNA replication machinery by ubiquitin and SUMO plays key roles in the faithful duplication of the genetic information. Among other functions, ubiquitination and SUMOylation serve as signals for the extraction of factors from chromatin by the AAA ATPase VCP. In addition to the regulation of DNA replication initiation and elongation, we now know that ubiquitination mediates the disassembly of the replisome after DNA replication termination, a process that is essential to preserve genomic stability. Here, we review the recent evidence showing how active DNA replication restricts replisome ubiquitination to prevent the premature disassembly of the DNA replication machinery. Ubiquitination also mediates the removal of the replisome to allow DNA repair. Further, we discuss the interplay between ubiquitin-mediated replisome disassembly and the activation of CDK1 that is required to set up the transition from the S phase to mitosis. We propose the existence of a ubiquitin–CDK1 relay, where the disassembly of terminated replisomes increases CDK1 activity that, in turn, favors the ubiquitination and disassembly of more replisomes. This model has important implications for the mechanism of action of cancer therapies that induce the untimely activation of CDK1, thereby triggering premature replisome disassembly and DNA damage. Full article
(This article belongs to the Special Issue The Role of Post-translational Modifications in Chromatin and Cancer)
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