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One example are histone posttranslational modifications (PTMs), such as acetylation, methylation, phosphorylation and ubiquitination... These marks function as signals during various chromatin-based processes and act as platforms for recruitment, assembly or retention of chromatin-associated factors... The key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis are discussed... This finding revealed a novel function of the C1/C2 heterotetramer and highlighted the biological importance of RNA recognition by length... In a recent Point-of-View, Dr Ohno discusses questions raised by these results, together with some historical background of this finding (Fig.  3)... Dr Feng Gong and colleagues identified a deubiquitinating enzyme, USP24, as a likely DDB2-interacting protein... Interaction between DDB2 and USP24 was confirmed by co-precipitation... Importantly, knockdown of USP24 in two human cell lines decreased the steady-state levels of DDB2, indicating that USP24-mediated DDB2 deubiquitination prevents DDB2 degradation... In addition, the authors demonstrated that USP24 can cleave an ubiquitinated form of DDB2 in vitro... Taken together, these results suggest that the ubiquitin-specific protease USP24 is a novel regulator of DDB2 stability (Fig.  4).

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Figure 1. Cover of Epigenetics Volume 7, Issue 10 (October 2012).
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Figure 1: Figure 1. Cover of Epigenetics Volume 7, Issue 10 (October 2012).

Mentions: Different mechanisms exist to modify chromatin compaction, thereby allowing to control DNA accessibility. One example are histone posttranslational modifications (PTMs), such as acetylation, methylation, phosphorylation and ubiquitination. These marks function as signals during various chromatin-based processes and act as platforms for recruitment, assembly or retention of chromatin-associated factors. A recent Review by Dr Jacques Côté and coworkers focuses specifically on the regulation and functions of histone phosphorylation. The authors summarize the current knowledge of histone phosphorylation and describe the many kinases and phosphatases that regulate it. The key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis are discussed. Additionally, the authors describe the intricate crosstalk that occurs between phosphorylation and other histone modifications and contributes to the sophisticated control of the chromatin remodeling processes (Fig. 1).1


Landes Highlights
Figure 1. Cover of Epigenetics Volume 7, Issue 10 (October 2012).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3585020&req=5

Figure 1: Figure 1. Cover of Epigenetics Volume 7, Issue 10 (October 2012).
Mentions: Different mechanisms exist to modify chromatin compaction, thereby allowing to control DNA accessibility. One example are histone posttranslational modifications (PTMs), such as acetylation, methylation, phosphorylation and ubiquitination. These marks function as signals during various chromatin-based processes and act as platforms for recruitment, assembly or retention of chromatin-associated factors. A recent Review by Dr Jacques Côté and coworkers focuses specifically on the regulation and functions of histone phosphorylation. The authors summarize the current knowledge of histone phosphorylation and describe the many kinases and phosphatases that regulate it. The key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis are discussed. Additionally, the authors describe the intricate crosstalk that occurs between phosphorylation and other histone modifications and contributes to the sophisticated control of the chromatin remodeling processes (Fig. 1).1

View Article: PubMed Central

AUTOMATICALLY GENERATED EXCERPT
Please rate it.

One example are histone posttranslational modifications (PTMs), such as acetylation, methylation, phosphorylation and ubiquitination... These marks function as signals during various chromatin-based processes and act as platforms for recruitment, assembly or retention of chromatin-associated factors... The key roles played by this histone mark in DNA repair, transcription and chromatin compaction during cell division and apoptosis are discussed... This finding revealed a novel function of the C1/C2 heterotetramer and highlighted the biological importance of RNA recognition by length... In a recent Point-of-View, Dr Ohno discusses questions raised by these results, together with some historical background of this finding (Fig.  3)... Dr Feng Gong and colleagues identified a deubiquitinating enzyme, USP24, as a likely DDB2-interacting protein... Interaction between DDB2 and USP24 was confirmed by co-precipitation... Importantly, knockdown of USP24 in two human cell lines decreased the steady-state levels of DDB2, indicating that USP24-mediated DDB2 deubiquitination prevents DDB2 degradation... In addition, the authors demonstrated that USP24 can cleave an ubiquitinated form of DDB2 in vitro... Taken together, these results suggest that the ubiquitin-specific protease USP24 is a novel regulator of DDB2 stability (Fig.  4).

No MeSH data available.