MBD2 and MBD3: elusive functions and mechanisms
Deoxyribonucleic acid methylation is a long known epigenetic mark involved in many biological processes and the ‘readers’ of this mark belong to several distinct protein families that ‘read’ and ‘translate’ the methylation mark into a function. Methyl-CpG binding domain proteins belong to one of the...
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| Format: | Online |
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Frontiers Media S.A.
2014
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4260518/ |
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pubmed-42605182014-12-23 MBD2 and MBD3: elusive functions and mechanisms Menafra, Roberta Stunnenberg, Hendrik G. Genetics Deoxyribonucleic acid methylation is a long known epigenetic mark involved in many biological processes and the ‘readers’ of this mark belong to several distinct protein families that ‘read’ and ‘translate’ the methylation mark into a function. Methyl-CpG binding domain proteins belong to one of these families that are associated with transcriptional activation/repression, regulation of chromatin structure, pluripotency, development, and differentiation. Discovered decades ago, the systematic determination of the genomic binding sites of these readers and their epigenome make-up at a genome-wide level revealed the tip of the functional iceberg. This review focuses on two members of the methyl binding proteins, namely MBD2 and MBD3 that reside in very similar complexes, yet appear to have very different biological roles. We provide a comprehensive comparison of their genome-wide binding features and emerging roles in gene regulation. Frontiers Media S.A. 2014-12-09 /pmc/articles/PMC4260518/ /pubmed/25538734 http://dx.doi.org/10.3389/fgene.2014.00428 Text en Copyright © 2014 Menafra and Stunnenberg. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Menafra, Roberta Stunnenberg, Hendrik G. |
| spellingShingle |
Menafra, Roberta Stunnenberg, Hendrik G. MBD2 and MBD3: elusive functions and mechanisms |
| author_facet |
Menafra, Roberta Stunnenberg, Hendrik G. |
| author_sort |
Menafra, Roberta |
| title |
MBD2 and MBD3: elusive functions and mechanisms |
| title_short |
MBD2 and MBD3: elusive functions and mechanisms |
| title_full |
MBD2 and MBD3: elusive functions and mechanisms |
| title_fullStr |
MBD2 and MBD3: elusive functions and mechanisms |
| title_full_unstemmed |
MBD2 and MBD3: elusive functions and mechanisms |
| title_sort |
mbd2 and mbd3: elusive functions and mechanisms |
| description |
Deoxyribonucleic acid methylation is a long known epigenetic mark involved in many biological processes and the ‘readers’ of this mark belong to several distinct protein families that ‘read’ and ‘translate’ the methylation mark into a function. Methyl-CpG binding domain proteins belong to one of these families that are associated with transcriptional activation/repression, regulation of chromatin structure, pluripotency, development, and differentiation. Discovered decades ago, the systematic determination of the genomic binding sites of these readers and their epigenome make-up at a genome-wide level revealed the tip of the functional iceberg. This review focuses on two members of the methyl binding proteins, namely MBD2 and MBD3 that reside in very similar complexes, yet appear to have very different biological roles. We provide a comprehensive comparison of their genome-wide binding features and emerging roles in gene regulation. |
| publisher |
Frontiers Media S.A. |
| publishDate |
2014 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4260518/ |
| _version_ |
1613165668898701312 |