Checkpoints meet the transcription at a novel histone milestone (H3-T11)

Shimada, Midori; Nakanishi, Makoto

doi:10.4161/cc.7.11.6062

Cited by 12 publications

(16 citation statements)

References 39 publications

(42 reference statements)

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“…Phosphorylation of H3T11 by Checkpoint kinase 1 (Chk1), possibly enhancing the recruitment to chromatin of the GCN5 histone acetyltransferase, also appears to be involved in the activation of the cyclin B1 and cdk1 promoters. 40,49 Intriguingly, demethylation of H3K9me3 by JMJD2A, a close homolog of JMJD2C, is blocked by phosphorylation of H3S10. 50 Thus, in metazoa, histone H3 phosphorylation can result in transcriptional activation by different mechanisms, depending on the particular modified residue (Fig.…”

Section: Histone H3 Phosphorylation During Interphasementioning

confidence: 99%

“…A number of protein kinases have been implicated in H3S10 phosphorylation in interphase cells of metazoa, such as Ribosomal Protein S6 Kinase (RPS6K) family members (MSK1, MSK2 and JIL-1), IκB Kinase α, PDZ binding kinase, the proto-oncogenic PIM1 and Transglutaminase 2. 2,10,35,37,40 With the exception of RPS6K family members, most of the metazoan kinases phosphorylating H3S10 do not appear to be conserved in the plant lineage. 16 Interestingly, environmental stresses enhance the activity of two A. thaliana RPS6K homologs 41 and, in both tobacco and A. thaliana cell lines, H3S10 phosphorylation has been observed to increase in response to high salinity or cold treatment.…”

Section: Histone H3 Phosphorylation During Mitosismentioning

confidence: 99%

“…Phosphorylation of H3T11, mediated by Protein kinase C Related Kinase 1 (PRK1), has been implicated in this type of transcriptional regulation. 40,47 and plants. However, the chromosomal localization, the timing and the putative functional significance of these phosphorylation events, with the possible exception of H3T3ph, seem to have diverged substantially.…”

Section: Histone H3 Phosphorylation During Mitosismentioning

confidence: 99%

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Histone H3 phosphorylation: Universal code or lineage specific dialects?

Cerutti¹,

Casas-Mollano²

2009

Epigenetics

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Post-translational modifications of histones modulate the functional landscape of chromatin and impinge on many DNA-mediated processes. Phosphorylation of histone H3 plays a role in the regulation of gene expression and in chromosome condensation/ segregation. Certain evolutionarily conserved residues on histone H3, namely Thr3, Ser10, Thr11 and Ser28, are phosphorylated during interphase or mitosis in both metazoa and plants. However, many of the kinases involved in these events appear to have evolved independently in different lineages. Likewise, the mechanistic function of specific phosphorylated amino acids, although poorly understood, also seems to differ among eukaryotes. Moreover, some modifications, such as phosphorylation of histone H3 Ser10, appear to have both a positive and a negative connotation and only become meaningful in combination with other histone marks within a particular chromatin context. Thus, a detailed understanding of the influence of histone H3 phosphorylation on biological processes may require learning organismal dialects of the histone code.

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Section: Histone H3 Phosphorylation During Interphasementioning

confidence: 99%

Section: Histone H3 Phosphorylation During Mitosismentioning

confidence: 99%

Section: Histone H3 Phosphorylation During Mitosismentioning

confidence: 99%

See 1 more Smart Citation

Histone H3 phosphorylation: Universal code or lineage specific dialects?

Cerutti¹,

Casas-Mollano²

2009

Epigenetics

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“…Recently, Lunardi et al showed transcriptional repression of Chk1 through oncogenic E26 transformation-specific (ETS) transcription factors in prostate cancer, which resulted in reduced Chk1 levels and unrepaired DNA damage [34]. Moreover, DNA damage induces dissociation of activated Chk1 from chromatin, thereby reducing phosphorylation of H3 T11 , resulting in the decreased levels of chromatin-bound GCN5 and Ac-H3 K9 , which led to transcriptional repression [21, 23]. …”

Section: Discussionmentioning

confidence: 99%

Chk1 Promotes DNA Damage Response Bypass following Oxidative Stress in a Model of Hydrogen Peroxide‐Associated Ulcerative Colitis through JNK Inactivation and Chromatin Binding

Reißig

Silver

Hartig

et al. 2017

Oxidative Medicine and Cellular Longevity

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Dysregulation of c-Jun N-terminal kinase (JNK) activation promoted DNA damage response bypass and tumorigenesis in our model of hydrogen peroxide-associated ulcerative colitis (UC) and in patients with quiescent UC (QUC), UC-related dysplasia, and UC-related carcinoma (UC-CRC), thereby adapting to oxidative stress. In the UC model, we have observed features of oncogenic transformation: increased proliferation, undetected DNA damage, and apoptosis resistance. Here, we show that Chk1 was downregulated but activated in the acute and quiescent chronic phases. In both phases, Chk1 was linked to DNA damage response bypass by suppressing JNK activation following oxidative stress, promoting cell cycle progression despite DNA damage. Simultaneously, activated Chk1 was bound to chromatin. This triggered histone acetylation and the binding of histone acetyltransferases and transcription factors to chromatin. Thus, chromatin-immobilized activated Chk1 executed a dual function by suppressing DNA damage response and simultaneously inducing chromatin modulation. This caused undetected DNA damage and increased cellular proliferation through failure to transmit the appropriate DNA damage signal. Findings in vitro were corroborated by chromatin accumulation of activated Chk1, Ac-H3, Ac-H4, and c-Jun in active UC (AUC) in vivo. Targeting chromatin-bound Chk1, GCN5, PCAF, and p300/CBP could be a novel therapeutic strategy to prevent UC-related tumor progression.

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“…Furthermore, subcellular localization of Chk1 is altered upon phosphorylation, allowing Chk1-mediated phosphorylation of important cell cycle modulators including p53 and Cdc25 phosphatases. This triggers multiple downstream events such as cell cycle arrest, and transcriptional repression [3–5]. Chk1 is thus essential for the S-phase, and G2, DNA damage checkpoints [6–8]; and also DNA replication checkpoints [9, 10].…”

Section: Introductionmentioning

confidence: 99%

The G2 checkpoint inhibitor CBP-93872 increases the sensitivity of colorectal and pancreatic cancer cells to chemotherapy

et al. 2017

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CBP-93872 suppresses maintenance of DNA double-stranded break-induced G2 checkpoint, by inhibiting the pathway between ataxia-telangiectasia mutated (ATM) and ATM- and Rad3-related (ATR) activation. To examine the potential use of CBP-93872 for clinical applications, we analyzed the synergistic effects of platinum-containing drugs, oxaliplatin and cisplatin, pyrimidine antimetabolites, gemcitabine and 5-fluorouracil (5-FU), in combination with CBP-93872, on cell lethality in colorectal and pancreatic cancer cell lines. Treatment with CBP-93872 significantly increased cancer cell sensitivities to various chemotherapeutic agents tested through suppression of checkpoint activation. Our results thus reveal that combination treatment of CBP-93872 with known chemotherapeutic agents inhibits phosphorylation of ATR and Chk1, and induces cell death.

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Checkpoints meet the transcription at a novel histone milestone (H3-T11)

Cited by 12 publications

References 39 publications

Histone H3 phosphorylation: Universal code or lineage specific dialects?

Histone H3 phosphorylation: Universal code or lineage specific dialects?

Chk1 Promotes DNA Damage Response Bypass following Oxidative Stress in a Model of Hydrogen Peroxide‐Associated Ulcerative Colitis through JNK Inactivation and Chromatin Binding

The G2 checkpoint inhibitor CBP-93872 increases the sensitivity of colorectal and pancreatic cancer cells to chemotherapy

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