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. 2011 Feb;32(2):139-40.
doi: 10.1038/aps.2011.3.

Ubiquitination/deubiquitination and acetylation/deacetylation: making DNMT1 stability more coordinated

Qi Hong  1 , Zhi-ming Shao
Affiliations

Ubiquitination/deubiquitination and acetylation/deacetylation: making DNMT1 stability more coordinated

Qi Hong et al. Acta Pharmacol Sin. 2011 Feb.
No abstract available

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Figures

Figure 1
Figure 1
A model of posttranslational regulation of DNMT1 stability. DNMT1 physically interacts with HAUSP, Tip60, UHRF1, HDAC1, and PCNA on chromatin. After the completion of DNA methylation in S phase, HAUSP dissociates from DNMT1 to enable DNMT1 degradation. Moreover, increased abundance of Tip60 results in increased acetylation of DNMT1, which in turn triggers the ubiquitination of DNMT1 by UHRF1. This sequence of events results in proteasomal degradation of DNMT1. In contrast, HAUSP and HDAC1 protect DNMT1 from degradation through deubiquitination and deacetylation, respectively. Reprinted with permission from AAAS: Science Signaling, copyright 2010.
See this image and copyright information in PMC

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