Sylvette CHASSEROT-GOLAZ PhD Biochemistry

Course and current status

Date of birth: 21-08-1959 à Montbéliard (FRANCE)


1985    : PhD from Université Louis Pasteur Option Biochimie et Biologie Moléculaire, IBMC Laboratoire de Biochimie Directeur Prof. J.P. Ebel

2005    : HDR from l'Université de Strasbourg

 Profesional experience

1988-1992: CR2 Inserm at IBMC UPR9002 (Director Prof. J.P. Ebel )

1993-2000: CR1 Inserm in  l’Unité Inserm U-338 (Director  D. Aunis)

 Actual function

CRHC  Inserm in the team "Intracellular membrane trafficking in the nervous and neuroendocrine "  in the UPR 3212 CNRS/Université de Strasbourg directed by S Gasman and N Vitale

Scientific Director of the platform   Imagerie in Vitro of  ITI Neurostra Strasbourg

Scientific summary

Exocytosis is a fundamental biological process, which ensures many cellular functions, including the secretion of chemical compounds. In neuroendocrine cells such as chromaffin cells, catecholamine secretion is calcium-regulated, and requires a concerted action of a number of proteins and lipids.

The aim of my research is to extend our understanding of the mechanisms governing regulated exocytosis in neuroendocrine cells. I am focusing on the role of Annexin A2 (ANXA2) a protein which bind phospholipids and actin in the presence of calcium. In chromaffin cells, ANXA2 is present either as a monomer or as a tetramer, associated with the protein S100A10. My previous work has shown that ANXA2 translocation to the plasma membrane is essential for exocytosis and that ANXA2 is involved in the membranr remodeling at exocytotic sites. Our results also suggest that S100A10 binds VAMP2 at plasma membrane in resting conditions. S100A10 would allow the recruitment in the presence of calcium and   close to the SNARE complex, of ANXA2, in order  to form lipid domains enriched in PIP2 and necessary to the formation of  SNARE complex at the fusion stage.

My project is to understand how ANXA2 alters the structure of the plasma membrane. Two directions will be explored: does ANXA2 directly aggregate lipids or does it complex with F-actin and change the mobility of lipids? The role of ANXA2 and membrane remodeling will also be addressed in the mechanisms of neurotransmission, synaptic plasticity and pain.

Elucidating the role of ANXA2 in the formation of lipid domains will complet our knowledge of the mechanisms regulating neuroendocrine secretion and neurotransmission and more generally the mechanisms underlying remodeling of biological membranes remodeling. The involvement of ANXA2 in lipid rafts formation of has been reported in several diseases such as Alzheimer's disease. Determining the mode of action of ANXA2 may provide a partial explanation of how certain neurodegenerative diseases develop.

Recently I have developed a new axe of research concerning the role  of endoplasmic reticulum membrane contact sites during exocytosis in neuroendocrine cells. I will focus on the characterization of ER-PM contacts near exocytotic sites in chromaffin cells. Considering that these structures are places of exchange of lipids and small molecules such as calcium. We will try to answer the following question: Do these RE-MP contacts participate in the supply of certain lipids such as phosphatidic acid or PIP2 necessary for the docking and fusion of the granules of secretions or for the regulation of calcium concentrations at exocytosis sites?

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