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Regulation of protein stability of DNA methyltransferase 1 by post-translational modifications

Regulation of protein stability of DNA methyltransferase 1 by post-translational modifications
Regulation of protein stability of DNA methyltransferase 1 by post-translational modifications
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.
DNA (cytosine-5-)-methyltransferase, epi-genetics, protein stability, post-translational modification, neoplasms
199-203
Scott, A.
ecc892d7-6f69-4d75-8e9c-02202e62cdd7
Song, J.
e82ff981-9c67-4ff5-8971-cb518bd1b3db
Ewing, R.
022c5b04-da20-4e55-8088-44d0dc9935ae
Wang, Z.
8983928f-aca4-4b48-a71b-959646c6aa77
Scott, A.
ecc892d7-6f69-4d75-8e9c-02202e62cdd7
Song, J.
e82ff981-9c67-4ff5-8971-cb518bd1b3db
Ewing, R.
022c5b04-da20-4e55-8088-44d0dc9935ae
Wang, Z.
8983928f-aca4-4b48-a71b-959646c6aa77

Scott, A., Song, J., Ewing, R. and Wang, Z. (2014) Regulation of protein stability of DNA methyltransferase 1 by post-translational modifications. [in special issue: Cancer] Acta Biophysica Sinica, 46 (3), 199-203. (doi:10.1093/abbs/gmt146). (PMID:24389641)

Record type: Article

Abstract

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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More information

Accepted/In Press date: 4 December 2013
e-pub ahead of print date: 3 January 2014
Published date: March 2014
Keywords: DNA (cytosine-5-)-methyltransferase, epi-genetics, protein stability, post-translational modification, neoplasms
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 377129
URI: http://eprints.soton.ac.uk/id/eprint/377129
PURE UUID: fc7f617c-22a1-4842-9547-e4af42da9b5a
ORCID for R. Ewing: ORCID iD orcid.org/0000-0001-6510-4001

Catalogue record

Date deposited: 26 May 2015 10:55
Last modified: 05 Nov 2019 01:38

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