The Language of Histone Crosstalk

Lee, Jung Shin; Smith, Edwin R.; Shilatifard, Ali

doi:10.1016/j.cell.2010.08.011

Cited by 542 publications

(418 citation statements)

References 22 publications

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“…In contrast, dDsk2 depletion induces a strong reduction of H3K4me3 at promoters (Fig. 7d), as expected from the reported H2Bub1-H3K4me3 crosstalk [29][30][31] . Notably, codepletion of Ubp8/Nonstop, which rescues H2Bub1 and expression (Fig.…”

supporting

confidence: 86%

“…8c,d). In this regard, it must be noted that dBre1 travels with the elongating RNA pol II along coding regions to induce H2Bub1, which stimulates FacilitatesChromatin-Transcription (FACT) activity and, thus, facilitates elongation [29][30][31]53 . On the other hand, dUbp8/Nonstop activity is mainly restricted to promoters since its depletion in dBre1-deficient cells has little effect in H2Bub1 levels at coding regions ( Supplementary Fig.…”

Section: Discussionmentioning

confidence: 99%

“…We also show that, through the UBA domain, dDsk2 interacts with monoubiquitylated H2B (H2Bub1), an abundant histone modification 28 that is induced at promoters during transcription initiation by an activator-mediated recruitment of the ubiquitin E2/E3 enzymes Rad6/Bre1 and stimulates additional epigenetic modifications required for transcription, such as H3K4me3 and H3K79me3 (reviewed in refs [29][30][31]. Later, during elongation, H2Bub1 extends along the entire coding region and facilitates progression of RNA pol II through chromatin.…”

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confidence: 86%

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dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

et al. 2015

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dDsk2 is a conserved extraproteasomal ubiquitin receptor that targets ubiquitylated proteins for degradation. Here we report that dDsk2 plays a nonproteolytic function in transcription regulation. dDsk2 interacts with the dHP1c complex, localizes at promoters of developmental genes and is required for transcription. Through the ubiquitin-binding domain, dDsk2 interacts with H2Bub1, a modification that occurs at dHP1c complex-binding sites. H2Bub1 is not required for binding of the complex; however, dDsk2 depletion strongly reduces H2Bub1. Co-depletion of the H2Bub1 deubiquitylase dUbp8/Nonstop suppresses this reduction and rescues expression of target genes. RNA polymerase II is strongly paused at promoters of dHP1c complex target genes and dDsk2 depletion disrupts pausing. Altogether, these results suggest that dDsk2 prevents dUbp8/Nonstop-dependent H2Bub1 deubiquitylation at promoters of dHP1c complex target genes and regulates RNA polymerase II pausing. These results expand the catalogue of nonproteolytic functions of ubiquitin receptors to the epigenetic regulation of chromatin modifications.

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confidence: 86%

Section: Discussionmentioning

confidence: 99%

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confidence: 86%

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dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

et al. 2015

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“…A nucleosome is a single unit of chromatin comprising 146 base pairs of DNA wrapped around histone octamers. The histone N-terminal tails are subjected to various post-translational modifications, including acetylation, methylation, phosphorylation, ubiquitination, and sumoylation [1,2]. Histone acetyltransferase (HAT) catalyzes the acetylation of core histones through the addition of an acetyl group from the pseudo-substrate acetyl coenzyme A (acetylCoA) to the lysine residue on the ε-amino group on the Nterminal of histones.…”

Section: Introductionmentioning

confidence: 99%

Acetyltransferases (HATs) as Targets for Neurological Therapeutics

et al. 2013

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The acetylation of histone and non-histone proteins controls a great deal of cellular functions, thereby affecting the entire organism, including the brain. Acetylation modifications are mediated through histone acetyltransferases (HAT) and deacetylases (HDAC), and the balance of these enzymes regulates neuronal homeostasis, maintaining the pre-existing acetyl marks responsible for the global chromatin structure, as well as regulating specific dynamic acetyl marks that respond to changes and facilitate neurons to encode and strengthen longterm events in the brain circuitry (e.g., memory formation). Unfortunately, the dysfunction of these finely-tuned regulations might lead to pathological conditions, and the deregulation of the HAT/HDAC balance has been implicated in neurological disorders. During the last decade, research has focused on HDAC inhibitors that induce a histone hyperacetylated state to compensate acetylation deficits. The use of these inhibitors as a therapeutic option was efficient in several animal models of neurological disorders. The elaboration of new cell-permeant HAT activators opens a new era of research on acetylation regulation. Although pathological animal models have not been tested yet, HAT activator molecules have already proven to be beneficial in ameliorating brain functions associated with learning and memory, and adult neurogenesis in wild-type animals. Thus, HAT activator molecules contribute to an exciting area of research.

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“…Chen and Allfrey (15) were the first to provide a correlation between alterations in chromatin architecture, histone acetylation, and PRG (c-fos and c-myc) transcription. Since then, numerous studies have addressed specific chromatin changes in eukaryotic genes, including PRGs (42)(43)(44)(45). Although the mRNA-encoding PRGs usually constitute ϳ1% of the total message in the growing cell, they are necessary to drive cells to re-enter the cell cycle (1).…”

Section: Discussionmentioning

confidence: 99%

Regulation of Primary Response Genes in B Cells

Fowler¹,

Suh

Buratowski

et al. 2013

Journal of Biological Chemistry

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Background: Primary response genes (PRGs) are important for proliferation and play a prominent role in B cell activation. Results: Distinct stimuli produce distinct modes of PRG regulation at the levels of both splicing and transcription. Conclusion: RNA maturation and splicing are regulated in a signal-specific manner. Significance: The nature of signaling controls the duration of transcriptional and splicing responses.

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The Language of Histone Crosstalk

Cited by 542 publications

References 22 publications

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

dDsk2 regulates H2Bub1 and RNA polymerase II pausing at dHP1c complex target genes

Acetyltransferases (HATs) as Targets for Neurological Therapeutics

Regulation of Primary Response Genes in B Cells

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