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MBD2 and MBD3: elusive functions and mechanisms.

Menafra R, Stunnenberg HG - Front Genet (2014)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Biology, Radboud University Nijmegen, Netherlands.

ABSTRACT
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.

No MeSH data available.


MBD3 binding to chromatin. (A) Schematic representation of MBD3 binding to unmethylated CGI promoters (B) MBD3 binding to unmethylated enhancers, that are in physical proximity to promoters in three-dimensional space. The question mark indicates the possible presence of other subunits involved in this association.
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Figure 3: MBD3 binding to chromatin. (A) Schematic representation of MBD3 binding to unmethylated CGI promoters (B) MBD3 binding to unmethylated enhancers, that are in physical proximity to promoters in three-dimensional space. The question mark indicates the possible presence of other subunits involved in this association.

Mentions: Taken together, the above findings suggest that MBD3 binds CpG-rich active promoters and enhancers that are not DNA methylated (Figure 3). The downstream functional consequence of MBD3 binding has still to be elucidated.


MBD2 and MBD3: elusive functions and mechanisms.

Menafra R, Stunnenberg HG - Front Genet (2014)

MBD3 binding to chromatin. (A) Schematic representation of MBD3 binding to unmethylated CGI promoters (B) MBD3 binding to unmethylated enhancers, that are in physical proximity to promoters in three-dimensional space. The question mark indicates the possible presence of other subunits involved in this association.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4260518&req=5

Figure 3: MBD3 binding to chromatin. (A) Schematic representation of MBD3 binding to unmethylated CGI promoters (B) MBD3 binding to unmethylated enhancers, that are in physical proximity to promoters in three-dimensional space. The question mark indicates the possible presence of other subunits involved in this association.
Mentions: Taken together, the above findings suggest that MBD3 binds CpG-rich active promoters and enhancers that are not DNA methylated (Figure 3). The downstream functional consequence of MBD3 binding has still to be elucidated.

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Department of Molecular Biology, Radboud University Nijmegen, Netherlands.

ABSTRACT
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.

No MeSH data available.