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MBD4 Interacts With and Recruits USP7 to Heterochromatic Foci
Author(s) -
Meng Huan,
Harrison David J.,
Meehan Richard R.
Publication year - 2015
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.25001
Subject(s) - microbiology and biotechnology , ubiquitin ligase , dnmt1 , biology , sumo protein , dna ligase , dna repair , ubiquitin , genetics , dna , methyltransferase , methylation , gene
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. J. Cell. Biochem. 116: 476–485, 2015. © 2014 The Authors. Journal of Cellular Biochemistry published by Wiley Periodicals, Inc.