Susanna Molinari
Susanna Molinari
affiliation: Università di Modena-Reggio Emilia
research area(s): Molecular Biology, Chemical Biology
Course: Molecular and Regenerative Medicine
University/Istitution: Università di Modena-Reggio Emilia
1991−1994. PhD training in Molecular and Cellular Biology and Pathology at the Department of Biomedical Science (University of Modena and Reggio Emilia).
July-September 1993 Visitor student in the laboratory of Dr P.C. Emson, MRC Molecular Neuroscience Group, Dept. of Neurobiology, AFRC Babraham Institute Babraham, Cambridge UK
1991 Degree in Pharmaceutical Sciences, mark 110/110 magna cum laude at the University of Modena and Reggio Emilia (Italy).
1990. Degree in Pharmaceutical Chemistry, mark 110/110 magna cum laude at the University of Modena and Reggio Emilia (Italy).
1999-today Researcher position at the Department of Biomedical Science, University of Modena and Reggio Emilia
1996-1999 Post doctoral research fellow at the Department of Molecular Biology, GMD Pasteur Institute Paris (France) in the laboratory of Margaret Buckingham.
Research activity focused on the molecular mechanisms governing myogenesis and particularly on the regulation of MEF2 family transcription factors in muscle cells.
Mechanisms that regulate the activity of the MEF2C transcription factor during skeletal myogenesis: 1) functional role of the interaction between phosphorylated MEF2C and the peptidil prolyl cis trans isomerase Pin1 in muscle cells and during myogenic development of the vertebrate Zebrafish in collaboration with the laboratory directed by Dr Simon M. Hughes (Randall Division of Cell and Molecular Biophysics, King’s College London UK); 2) identification of the signalling pathways responsible of the phosphorylation of MEF2C on the relevant Pin1 binding sites.
-Magli A, Angelelli C, Ganassi M, Baruffaldi F, Matafora V, Battini R, Bachi A, Messina G, Rustighi A, Del Sal G, Ferrari S, Molinari S.
Proline isomerase Pin1 represses terminal differentiation and myocyte enhancer factor 2C function in skeletal muscle cells.
J Biol Chem. 2010 Nov 5;285(45):34518-27.
- Angelelli C. Magli A., Ferrari D., Ganassi M., Matafora V., Parise F., Razzini G., Bachi A., Ferrari S., Molinari S.
Differentiation−dependent lysine 4 acetylation enhances MEF2C binding to DNA in skeletal muscle cells. Nucl. Acids Res. 2008; 36(3):915-28.
-Relaix F, Molinari S, Lemonnier M, Schafer B, Buckingham M.
The in vivo form of the murine class VI POU protein Emb is larger than that encoded by previously described transcripts. Gene. 2004 May 26;333:35-46.
-Molinari S, Relaix F, Lemonnier M, Kirschbaum B, Schafer B, Buckingham M.
A novel complex regulates cardiac actin gene expression through interaction of Emb, a class VI POU domain protein, MEF2D, and the histone transacetylase p300. Mol Cell Biol. 2004 Apr;24(7):2944-57.
Project Title:
Identification of the molecular partners of MEF2C in proliferating and differentiating skeletal muscle cells
The transcription factor MEF2C (Myocyte Enhancer Factor-2) is expressed in skeletal muscle cells both in proliferating myoblasts and differentiating myotubes. Although its role in promoting muscle cell specific gene expression is widely established, the function played by MEF2C in proliferating muscle cells is still obscure. With the aim of identifying the molecular pathways where MEF2C is involved, we envisage to identify its molecular partners by mass spectrometry analysis of the co-immunoprecipitated products in myoblasts and myotubes.