Histone modifications: Now summoning sumoylation

Nathan, Dafna; Sterner, David E.; Berger, Shelley L.

doi:10.1073/pnas.2436173100

Cited by 97 publications

(64 citation statements)

References 22 publications

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“…As a result, chromatin has to undergo a number of structural modifications for transcription to occur (Wolffe & Hayes 1999). Recent studies indicate that covalent modifications of histone tails -including acetylation, methylation, phosphorylation, ubiquitination, sumoylation, and poly-ADP-ribosylation -play a vital role in regulating chromatin structure dynamics and gene expression (Fischle et al 2003b, Nathan et al 2003. Modification of histones by ubiquitin has recently come to the forefront as a previously unrecognized level of transcriptional control (Jason et al 2002, Ulrich 2002, Muratani & Tansey 2003, Zhang 2003.…”

Section: Ubiquitin and Chromatin Structurementioning

confidence: 99%

Linking the ubiquitin–proteasome pathway to chromatin remodeling/modification by nuclear receptors

Kinyamu

Chen²,

Archer

2005

Journal of Molecular Endocrinology

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Over 25 years ago, eukaryotic cells were shown to contain a highly specific system for the selective degradation of short-lived proteins, this system is known as the ubiquitin-proteasome pathway. In this pathway, proteins are targeted for degradation by covalent modification by a small highly conserved protein named ubiquitin. Ubiquitin-mediated degradation of regulatory proteins plays an important role in numerous cell processes, including cell cycle progression, signal transduction and transcriptional regulation. Recent experiments have shown that the ubiquitin-proteasome pathway is also involved in nuclear hormone receptor (NR)-mediated transcriptional regulation. The idea that the ubiquitinproteasome pathway is involved in NR-mediated transcription is strengthened by experiments showing that ubiquitinproteasome components are recruited to NR target gene promoters. However, it is not clear how these components modulate NR-mediated chromatin remodeling and gene expression. In this review, we postulate the role of the ubiquitin-proteasome pathway on NR-mediated chromatin remodeling and gene regulation based on the current knowledge from studies implicating the pathway in chromatin structure modifications that are applicable to NR function. Since evidence from this laboratory, using the glucocorticoid receptor responsive mouse mammary tumor virus (MMTV) promoter organized as chromatin, suggest that the ubiquitin-proteasome system may be involved in the elongation phase of transcription, we particularly concentrate on chromatin modifications associated with the elongation phase.

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Section: Ubiquitin and Chromatin Structurementioning

confidence: 99%

Linking the ubiquitin–proteasome pathway to chromatin remodeling/modification by nuclear receptors

Kinyamu

Chen²,

Archer

2005

Journal of Molecular Endocrinology

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“…The histone tails, which constitute 30% of the nucleosomal mass, extend out of the nucleosome between the gyres of wrapped DNA and are platforms for a multitude of post-translational modifications (phosphorylation, poly-ADP-ribosylation, acetylation, methylation, ubiquitylation and sumoylation) (reviewed in [2,3]). It is postulated that combinations of such modifications generate an epigenetic "histone code" that is read by a variety of protein factors to control basic DNA processes [4,5].…”

Section: Introductionmentioning

confidence: 99%

cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines

Rodriguez-Collazo

Snyder

Chiffer

et al. 2008

Experimental Cell Research

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The phosphorylation of histone H3 is known to play a role in regulation of transcription as well as preparation of chromosomes for mitosis. Various signaling cascades induce H3 phosphorylation, particularly at genes activated by these pathways. In this study we show that signaling can also have the opposite effect. Activators of cAMP signaling induce a rapid and potent loss of H3 phosphorylation. This effect is not mediated through a cAMP metabolite since a membranepermeable form of AMP had no effect on H3 phosphorylation and a phosphodiesterase-resistant cAMP analog efficiently reduced it. cAMP is also the likely regulator of H3 phosphorylation under physiological conditions since only supra-pharmacological doses of cGMP induce the loss of H3 phosphorylation. The loss of phosphorylation is specific for histone H3 since we do not observe drastic losses in total phosphorylation of other histones. In addition, other H3 modifications are unaffected with the exception of lysine 9 methylation, which is elevated. Analysis of cell growth and cell cycle show that cAMP signaling inhibits cell growth and arrests cells at both G1 and G2/M. Similar effects of cAMP signaling on H3 phosphorylation are observed in a variety of mammary adenocarcinoma-derived cell lines. In syngeneic human breast derived cell lines, one diploid and non-transformed, the other derived from a ductal carcinoma, the loss of H3 phosphorylation is significantly more sensitive to cAMP concentration in the transformed cell line.

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“…Other epigenetic factors are useful for drug discovery, such as acetylation, methylation and phosphorylation, ubiquitination, sumoylation and ADP-ribosylation [112,113]. A list of these agents is summarised in Table 1a and Table 1b [114,115].…”

Section: Epigenetic Regulation and Drug Discoverymentioning

confidence: 99%

DNA Methylation in Mammalian Cells

Winata¹,

William²,

Keena³

et al. 2018

Gene Expression and Regulation in Mammalian Cells - Transcription Toward the Establishment of Novel Therapeutics

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Epigenetic regulation was first studied in the 1970s and has quickly gained global interest. It is involved at many different stages of mammalian cell development. The broad nature of epigenetic regulation has led to it being referred to as an 'all stage' mechanism of regulation as it is implicated in many developmental stages including embryonic development, ageing and in cancer progression. The term 'epigenetic' refers to the alteration of gene expression without changing the genomic sequence. Epigenetic regulation involves the main subtypes of DNA methylation and histone modification, and microRNA expression. Epigenetic alteration is used by mammalian cells to 'turn-on and -off' the gene expression. During embryonic development this process is used to induce cell apoptosis of genes that are no longer useful. During cancer development, epigenetics works to repress tumour suppressor gene expression and activate oncogene expression. The stability and sustainability for the detection of epigenetic markers make it an attractive area for biomarker and drug discovery. In this book chapter we will discuss the key epigenetic processes involved in mammalian cell development and disease progression, specifically in cancer.

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Histone modifications: Now summoning sumoylation

Cited by 97 publications

References 22 publications

Linking the ubiquitin–proteasome pathway to chromatin remodeling/modification by nuclear receptors

Linking the ubiquitin–proteasome pathway to chromatin remodeling/modification by nuclear receptors

cAMP signaling induces rapid loss of histone H3 phosphorylation in mammary adenocarcinoma-derived cell lines

DNA Methylation in Mammalian Cells

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