Journal
JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 116, Issue 3, Pages 476-485Publisher
WILEY
DOI: 10.1002/jcb.25001
Keywords
MBD4; UHRF1; USP7; HETEROCHROMATIN REPLICATION AND FORMATION
Categories
Funding
- MRC
- IMI-MARCAR
- BBSRC
- MRC [MC_PC_U127574433] Funding Source: UKRI
- Medical Research Council [MC_PC_U127574433] Funding Source: researchfish
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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. (C) 2014 Wiley Periodicals, Inc.
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