MBD4 interacts with and recruits USP7 to heterochromatic foci

H. Meng, D.J. Harrison, R.R. Meehan

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

MBD4 is the only methyl-CpG binding protein that possesses a C-terminal glycosylase domain. It has been associated with a number of nuclear pathways including DNA repair, DNA damage response, the initiation of apoptosis, transcriptional repression, and DNA demethylation. However, the precise contribution of MBD4 to these processes in development and relevant diseases remains elusive. We identified UHRF1 and USP7 as two new interaction partners for MBD4. Both UHRF1, a E3 ubiquitin ligase, and USP7, a de-ubiquinating enzyme, regulate the stability of the DNA maintenance methyltransferase, Dnmt1. The ability of MBD4 to directly interact with and recruit USP7 to chromocenters implicates it as an additional factor that can potentially regulate Dnmt1 activity during cell proliferation.
Original languageEnglish
Pages (from-to)476-485
Number of pages10
JournalJournal of Cellular Biochemistry
Volume116
Issue number3
Early online date20 Jan 2015
DOIs
Publication statusPublished - 1 Mar 2015

Keywords

  • MBD4
  • UHRF1
  • USP7
  • Heterochromatin replication and formation

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