Myocyte enhancer factor 2: Difference between revisions

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{{STRUCTURE_1tqe|  PDB=1tqe | SIZE=400| SCENE= |right|CAPTION=Mouse HDAC9 (brown and aquamarine) complex with myocyte-specific enhancer factor (blue, olive, green, light green) and DNA [[1tqe]] }}
<StructureSection load='1tqe' size='350' side='right' caption='Mouse HDAC9 (aquamarine) complex with myocyte-specific enhancer factor (green) and DNA (PDB entry [[1tqa]])' scene=''>


==Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure==
==Understanding of the Recruitment of HDACs by MEF2, Based on Their Structure==
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Additionally, by looking to the <scene name='Sandbox_Reserved_1/False_dimer/2'>structure</scene> obtained by X-ray crystallography, one could also think that complexes HDAC9/MEF2/DNA dimerize ''in vivo''. During the crystallization process, two complexes were contained in the same asymmetric unit, giving such a false impression. Thus, it is important to emphasize that the biological unit would be composed only by <scene name='Sandbox_Reserved_1/Complex/5'>a monomer of HDAC9, a dimer of MEF2 and a fragment of double strand DNA</scene>[http://www.ebi.ac.uk/pdbe/pqs/pqs-bin/macmol.pl?filename=1TQE].
Additionally, by looking to the <scene name='Sandbox_Reserved_1/False_dimer/2'>structure</scene> obtained by X-ray crystallography, one could also think that complexes HDAC9/MEF2/DNA dimerize ''in vivo''. During the crystallization process, two complexes were contained in the same asymmetric unit, giving such a false impression. Thus, it is important to emphasize that the biological unit would be composed only by <scene name='Sandbox_Reserved_1/Complex/5'>a monomer of HDAC9, a dimer of MEF2 and a fragment of double strand DNA</scene>[http://www.ebi.ac.uk/pdbe/pqs/pqs-bin/macmol.pl?filename=1TQE].
*'''MEF2A''' is a substrate for p38<ref>PMID:9858528</ref>.
*'''MEF2B''' and '''MEF2D''' are potent trans-activators expressed in early myogenic lineages<ref>PMID:8669199</ref>.
*'''MEF2C''' controls chondrocyte hypertrophy and bone development<ref>PMID:17336904</ref>.


== Disease ==
== Disease ==
High expression of MEF2C is observed in leukemia<ref>PMID:23435431</ref>.
High expression of MEF2C is observed in leukemia<ref>PMID:23435431</ref>.  Mutations in MEF2A are associated with coronary artery disease and myocardial infraction<ref>PMID:20031581</ref>.  Mutations in MEF2B are associated with non-hodgkin lymphoma<ref>PMID:26245647</ref>.


==Additional Resources==
==Additional Resources==
For Additional information, See [[Transcription and RNA Processing]]
For Additional information, See [[Transcription and RNA Processing]]
</StructureSection>
== 3D Structures of myocyte enhancer factor 2 ==


== 3D Structures of myocyn enhancer factor 2 ==
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[1egw]], [[1c7u]], [[3kov]] – hMEF2A N terminal + DNA – human<br />
[[1egw]], [[1c7u]], [[3kov]] – hMEF2A N terminal + DNA – human<br />
[[3mu6]] – hMEF2A N terminal (mutant) + DNA <br />
[[3mu6]] – hMEF2A N terminal (mutant) + DNA <br />
[[3p57]] – hMEF2A N terminal + DNA + histone acetyltransferase<br />
[[3p57]] – hMEF2A N terminal + DNA + histone acetyltransferase<br />
[[6c9l]] – hMEF2B <br />
[[1n6j]] – hMEF2B N terminal + DNA + calcineurin-binding protein<br />
[[1n6j]] – hMEF2B N terminal + DNA + calcineurin-binding protein<br />
[[1tqe]] – hMEF2B N terminal + DNA + histone deacylase 9 peptide<br />
[[1tqe]] – hMEF2B N terminal + DNA + histone deacylase 9 peptide<br />
[[6wc5]] – hMEF2B + NKX-2.5 + DNA<br />
[[7x1n]] – hMEF2D + DNA<br />
[[5f28]] – MEF2C N terminal + focal adhesion kinase 1 - mouse<br />
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]

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Ricardo Alchini, David Canner, Michal Harel, Jaime Prilusky