CHUV Centre Hospitalier Universitaire Vaudois
- Responsable scientifique de la plateforme Biobanque tissulaire et études cliniques
2016 - maintenant
UNIL, dpt de Pharmacologie et Toxicologie
- Responsable de Recherche
2014 - 2015
ISREC, Ecole Polytechnique Fédérale de Lausanne
- Collaborateur scientifique
2009 - 2013Project: Identification of target mRNAs of mouse Bicaudal-C
Summary:
The lab seeks to elucidate how morphogenesis and patterning are regulated in embryonic tissues, and how perturbations in such developmental programs affect tissue homeostasis and neoplastic growth. TGFß and Wnt signalling pathways are of particular interest, because they regulate the proliferation and differentiation of stem and progenitor cells in several embryonic and self-renewing adult tissues and during tumor progression. Yet, the molecular mechanisms which harness the oncogenic potential of such activities are poorly understood. The aim of the present project is to determine how Wnt signalling and possibly other morphogenetic activities are regulated by the conserved RNA-binding K-homology domain protein Bicaudal-C (BicC).
Publication:
Journal of Translational Medicine, 2015
"Urine Fetuin A is a biomarker of Autosomal Dominant Kidney Disease progression"
Nathalie Piazzon, Florian Bernet, Linda Guihard, Wouter Leonhard, Séverine Urfer, Dmitri Firsov, Hassib Chehade, Bruno Vogt, Sophia Pergiovani, Dorien Peters, Olivier Bonny, and Daniel B. Constam
Journal of Molecular Cell Biology, 2012
“Bicc1 links the regulation of cAMP signaling in polycystic kidneys to microRNA-induced silencing”
Nathalie Piazzon, Charlotte Maisonneuve, Isabelle Guilleret, Samuel Rotman, and Daniel B. Constam
Laboratoire MAEM UMR CNRS-UHP 7567
- Chercheur doctorant
2004 - 2008Project: Function of the Survival of Motor Neuron (SMN) complex in the biogenesis of RNA/protein particles
Summary:
Spinal muscular atrophy (SMA) is caused by reduced levels of the survival of motor neuron (SMN) protein. SMN protein is associated with the proteins Gemin 2 to 8 and unrip to form the SMN complex. Although the SMN protein is present in all cell types, SMA is restricted to a defect in motor neuron.The emerging picture is that the SMN complex acts as a macromolecular chaperone of RNPs to increase the efficiency and fidelity of RNA–protein interactions, and to provide an opportunity for these interactions to be regulated.
Publication:
Nucleic Acid Res., 2013
"Implication of the SMN complet in the biogenesis and steady state level of the signal recognition particle"
Nathalie Piazzon, Florence Schlotter, Suzie Lefebvre, Maxime Dodré, Agnès Mereau, Julien Soret, Aurore Besse, Martine Barkats, Rémi Bordonné, Christiane Branlant, and Séverine Massenet
J. Biol. Chem, 2008
“In vitro and in cellulo evidences for association of the Survival of Motor Neuron Complex with the Fragile X Mental Retardation Protein”
Piazzon N., Rage F., Schlotter F., Moine H., Branlant C. and Massenet S.
