Myocyte enhancer factor 2: Difference between revisions

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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 ==