The known DNA methyltransferases (DNMT1, DNMT3A, and DNMT3B) can be SUMOylated (reviewed in Xu et al. 2010, Denis et al. 2011). SUMOylation affects the catalytic activity of DNMT1 and the protein interactions of DNMT3A.
View original pathway at Reactome.
Lee B, Muller MT.; ''SUMOylation enhances DNA methyltransferase 1 activity.''; PubMedEurope PMCScholia
Park J, Kim TY, Jung Y, Song SH, Kim SH, Oh DY, Im SA, Bang YJ.; ''DNA methyltransferase 3B mutant in ICF syndrome interacts non-covalently with SUMO-1.''; PubMedEurope PMCScholia
Xu F, Mao C, Ding Y, Rui C, Wu L, Shi A, Zhang H, Zhang L, Xu Z.; ''Molecular and enzymatic profiles of mammalian DNA methyltransferases: structures and targets for drugs.''; PubMedEurope PMCScholia
Kang ES, Park CW, Chung JH.; ''Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1.''; PubMedEurope PMCScholia
Denis H, Ndlovu MN, Fuks F.; ''Regulation of mammalian DNA methyltransferases: a route to new mechanisms.''; PubMedEurope PMCScholia
DNMT3B is SUMOylated with SUMO1 at unknown lysine residues (Kang et al. 2001, Park et al. 2008). SUMOylation relieves transcriptional repression by DNMT3B.
As inferred from mouse homologs, CBX4 (Pc2) SUMOylates DNMT3A with SUMO1 at more than one lysine residue in the N-terminal (regulatory) domain. SUMOylation reduces the interaction of DNMT3A with HDAC1 and HDAC2.
Try the New WikiPathways
View approved pathways at the new wikipathways.org.Quality Tags
Ontology Terms
Bibliography
History
External references
DataNodes
Annotated Interactions