DNMT1 Stability Is Regulated by Proteins Coordinating Deubiquitination and Acetylation-Driven Ubiquitination

Zhanwen Du, Jing Song, Yong Wang, Yiqing Zhao, Kishore Guda, Shuming Yang, Hung-Ying Kao, Yan Xu, Joseph Willis, Sanford D. Markowitz, David Sedwick, Robert M. Ewing, Zhenghe Wang*

*To whom correspondence should be addressed. E-mail: zhenghe.wang{at}case.edu

This PDF file includes:

• Materials and Methods
• Fig. S1. Engineering of DNMT1, DNMT 3b, and Tip60 3xFlag-tagged knock-in cells.
• Fig. S2. Identification of HAUSP by LC-MS/MS.
• Fig. S3. Specific interaction between DNMT1 and HAUSP.
• Fig. S4. Physical interaction is required for HAUSP to deubiquitinate DNMT1.
• Fig. S5. HDAC inhibitors induce DNMT1 degradation.
• Fig. S6. DNMT1-interacting proteins associate with each other.
• Fig. S7. The abundance of DNMT1 changes during the cell cycle.
• Fig. S8. IHC staining of HAUSP and DNMT1 in normal colon tissues.
• Fig. S9. HDAC inhibitors induce apoptosis in HAUSP knockout cells.
• Fig. S10. DNA methylation status of wild-type and HAUSP knockout cells.
• Fig. S11. Quantification and statistical analysis of Western blots.

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