H4K20 methylation regulates quiescence and chromatin compaction

Evertts, Adam G.; Manning, Amity L.; Wang, Xin; Dyson, Nicholas J.; Garcia, Benjamin A.; Coller, Hilary A.

doi:10.1091/mbc.e12-07-0529

Cited by 129 publications

(127 citation statements)

References 69 publications

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“…This suggests that modifications on top of H3K4me3 are likely important in supporting PLOD2 transcriptional activation. Of interest is the decrease in H4K20me3, which is involved in heterochromatin formation (63,64), and the increase of H3K79me2, which is related to gene expression and transcription elongation (29,65). Although the precise roles of H3K79me2 and H4K20me3 in transcriptional regulation are still unclear, these modifications appear to be more associated with TGF␤1-induced PLOD2 expression than the classical marks H3K4me3, H3K9me3, and H3K27me3, which were not significantly affected by TGF␤1.…”

Section: Discussionmentioning

confidence: 99%

Procollagen Lysyl Hydroxylase 2 Expression Is Regulated by an Alternative Downstream Transforming Growth Factor β-1 Activation Mechanism

Gjaltema

Rond

Rots

et al. 2015

Journal of Biological Chemistry

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Background: PLOD2 expression and subsequent collagen pyridinoline cross-links are induced in fibrotic tissues by TGF␤1. Results: TGF␤1 induces changes to histone modifications. SP1 and SMAD3 but not P300/CBP are responsible for PLOD2 induction. Conclusion: SMAD3 regulates TGF␤1-induced PLOD2 expression via histone-modifying enzymes other than the currently known downstream effectors. Significance: Unraveling PLOD2 transcriptional regulation would provide new ways to interfere in fibrotic processes.

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Section: Discussionmentioning

confidence: 99%

Procollagen Lysyl Hydroxylase 2 Expression Is Regulated by an Alternative Downstream Transforming Growth Factor β-1 Activation Mechanism

Gjaltema

Rond

Rots

et al. 2015

Journal of Biological Chemistry

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“…Depending on the cell type, up to ϳ80% of H4 molecules can be dimethylated, whereas H4K20me1 and H4K20me3 are generally less abundant, for example being present on 10 and 5% of nucleosomes in asynchronous HeLa cells, respectively, with similar ratios observed in mouse embryonic fibroblasts (MEFs) and other cell types (13)(14)(15)(16). Three distinct SET domains containing lysine (K) methyltransferase (KMT) enzymes, SETD8 (SET8, PR-SET7), SUV4-20H1, and SUV4-20H2, are responsible for the generation of the three different methyl states of H4K20 (17)(18)(19)(20).…”

mentioning

confidence: 92%

Histone H4 Lysine 20 (H4K20) Methylation, Expanding the Signaling Potential of the Proteome One Methyl Moiety at a Time

Nuland

Gozani

2016

Molecular & Cellular Proteomics

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Covalent post-translational modifications (PTMs) of proteins can regulate the structural and functional state of a protein in the absence of primary changes in the underlying sequence. Common PTMs include phosphorylation, acetylation, and methylation. Histone proteins are critical regulators of the genome and are subject to a highly abundant and diverse array of PTMs. To highlight the functional complexity added to the proteome by lysine methylation signaling, here we will focus on lysine methylation of histone proteins, an important modification in the regulation of chromatin and epigenetic processes. We review the signaling pathways and functions associated with a single residue, H4K20, as a model chromatin and clinically important mark that regulates biological processes ranging from the DNA damage response and DNA replication to gene expression and silencing. Molecular

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“…Recent studies have described the properties of quiescent cells [7,3,8–12], including changes in gene expression patterns [13–19], but more research is required to truly understand the molecular basis of quiescence. This leads to the question: What approaches are available to ascertain whether a cell is in a quiescent state using different cell-based techniques?…”

Section: Introductionmentioning

confidence: 99%

An In Vitro Model of Cellular Quiescence in Primary Human Dermal Fibroblasts

Mitra

Coller

2017

Methods in Molecular Biology

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Cellular quiescence is a reversible mode of cell cycle exit that allows cells and organisms to withstand unfavorable stress conditions. The factors that underlie the entry, exit, and maintenance of the quiescent state are crucial for understanding normal tissue development and function as well as pathological conditions such as chronic wound healing and cancer. In vitro models of quiescence have been used to understand the factors that contribute to quiescence under well-controlled experimental conditions. Here we describe an in vitro model of quiescence that is based on neonatal human dermal fibroblasts. The fibroblasts are induced into quiescence by antiproliferative signals contact inhibition and serum-starvation (mitogen withdrawal). We describe the isolation of fibroblasts from skin, methods for inducing quiescence in isolated fibroblasts, and approaches to manipulate the fibroblasts in proliferating and quiescent states in order to determine critical regulators of quiescence.

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H4K20 methylation regulates quiescence and chromatin compaction

Cited by 129 publications

References 69 publications

Procollagen Lysyl Hydroxylase 2 Expression Is Regulated by an Alternative Downstream Transforming Growth Factor β-1 Activation Mechanism

Procollagen Lysyl Hydroxylase 2 Expression Is Regulated by an Alternative Downstream Transforming Growth Factor β-1 Activation Mechanism

Histone H4 Lysine 20 (H4K20) Methylation, Expanding the Signaling Potential of the Proteome One Methyl Moiety at a Time

An In Vitro Model of Cellular Quiescence in Primary Human Dermal Fibroblasts

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