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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 4. Cover of Cell Cycle Volume 11, Issue 23 (December 1, 2012).
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Figure 4: Figure 4. Cover of Cell Cycle Volume 11, Issue 23 (December 1, 2012).

Mentions: Nucleotide excision repair (NER) is the major pathway for repair of UV-induced cyclobutane pyrimidine dimers (CPDs) in human cells. Damage-specific DNA-binding protein 2 (DDB2) was first isolated as a subunit of the UV-DDB heterodimeric complex that is involved in DNA damage recognition in the NER pathway. DDB2 is required for efficient repair of CPDs in chromatin and is a component of the CUL4-RING E3 ubiquitin ligase complex (CRL4DDB2) that targets XPC protein, histones and DDB2 itself for ubiquitination. Recently, a yeast two-hybrid screen of a human cDNA library was performed to identify potential DDB2 partners. 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).4


Landes Highlights
Figure 4. Cover of Cell Cycle Volume 11, Issue 23 (December 1, 2012).
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 4: Figure 4. Cover of Cell Cycle Volume 11, Issue 23 (December 1, 2012).
Mentions: Nucleotide excision repair (NER) is the major pathway for repair of UV-induced cyclobutane pyrimidine dimers (CPDs) in human cells. Damage-specific DNA-binding protein 2 (DDB2) was first isolated as a subunit of the UV-DDB heterodimeric complex that is involved in DNA damage recognition in the NER pathway. DDB2 is required for efficient repair of CPDs in chromatin and is a component of the CUL4-RING E3 ubiquitin ligase complex (CRL4DDB2) that targets XPC protein, histones and DDB2 itself for ubiquitination. Recently, a yeast two-hybrid screen of a human cDNA library was performed to identify potential DDB2 partners. 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).4

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.