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. 2015 Mar 19;14(10):1517–1528. doi: 10.1080/15384101.2015.1026519

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Sara Badodi, Fiorenza Baruffaldi, Massimo Ganassi, Renata Battini, and Susanna Molinari

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 4. — Ser98/Ser110 phosphorylation and a proximal conserved D-box are required for CDC20-dependent degradation of MEF2C. (A) Amminoacid sequence encoded by the α1 isoform. Sequence of a putative D-box near the Ser98 and Ser110 phosphoacceptor sites. Alignment with ClustalW of the amminoacid sequences encompassing the phosphorylable residues of MEF2C proteins from different species revealed the presence of a conservd D-box. Amminoacids forming the putative destruction box (D-box) are highlighted in blue, Ser98 and Ser110 in red. The deletion introduced in the MEF2C D-box mutant (MEF2C D-box del) is indicated. (B) The D-box and Ser98/Ser110 phosphorylation are all necessary for MEF2C degradation. C2 proliferating myoblasts were co-transfected with an empty vector (EV) or HA-tagged CDC20 and CDH1 vectors along with, alternatively the wild type MEF2C protein (WT), the D-box deleted mutant (WT D-box DEL), the not-phosphorylable MEF2C 2SA mutant or the MEF2C 2SA mutant deleted of the D-box (2SA D-box DEL). Cell extracts were analyzed by Western blotting with antibodies against FLAG and HA. Vinculin was used as loading control.