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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 Hong¹, Zhi-ming Shao

Affiliations

Affiliation

¹ Department of Breast Surgery, Breast Cancer Institute, Cancer Hospital, Institutes of Biomedical Science, Shanghai Medical College, Fudan University, Shanghai, China.

PMID: 21293465
PMCID: PMC4009943
DOI: 10.1038/aps.2011.3

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

Qi Hong et al. Acta Pharmacol Sin. 2011 Feb.

. 2011 Feb;32(2):139-40.

doi: 10.1038/aps.2011.3.

Authors

Qi Hong¹, Zhi-ming Shao

Affiliation

¹ Department of Breast Surgery, Breast Cancer Institute, Cancer Hospital, Institutes of Biomedical Science, Shanghai Medical College, Fudan University, Shanghai, China.

PMID: 21293465
PMCID: PMC4009943
DOI: 10.1038/aps.2011.3

No abstract available

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Figures

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.

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