Open AccessRegulation of protein stability of DNA methyltransferase 1 by post-translational modifications
Author(s) -
Anthony Scott,
Jing Song,
Rob M. Ewing,
Zhenghe Wang
Publication year - 2014
Publication title -
acta biochimica et biophysica sinica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.771
H-Index - 57
eISSN - 1745-7270
pISSN - 1672-9145
DOI - 10.1093/abbs/gmt146
Subject(s) - dnmt1 , epigenetics , dna methyltransferase , dna methylation , methyltransferase , biology , methylation , ubiquitin , acetylation , dna replication , epigenomics , microbiology and biotechnology , genetics , regulation of gene expression , dna , computational biology , gene , gene expression
DNA methylation is an important epigenetic mechanism that ensures correct gene expression and maintains genetic stability. DNA methyltransferase 1 (DNMT1) is the primary enzyme that maintains DNA methylation during replication. Dysregulation of DNMT1 is implicated in a variety of diseases. DNMT1 protein stability is regulated via various post-translational modifications, such as acetylation and ubiquitination, but also through protein-protein interactions. These mechanisms ensure DNMT1 is properly activated during the correct time of the cell cycle and at correct genomic loci, as well as in response to appropriate extracellular cues. Further understanding of these regulatory mechanisms may help to design novel therapeutic approaches for human diseases.
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