MBD4 interacts with and recruits USP7 to heterochromatic foci
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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.
Meng , H , Harrison , D J & Meehan , R R 2015 , ' MBD4 interacts with and recruits USP7 to heterochromatic foci ' Journal of Cellular Biochemistry , vol 116 , no. 3 , pp. 476-485 . DOI: 10.1002/jcb.25001
Journal of Cellular Biochemistry
Available under Open Access. This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record.
Work in R.M.'s lab is supported by the MRC, IMI-MARCAR and the BBSRC. H.M. was supported by British government overseas research funding and University of Edinburgh College of Medicine scholarships. D.J.H. is supported by EU FP7 CASyM programme.