Eric CHEVET
  • E-mail :[email]
  • Phone : +33 2 23 23 72 58
  • Location : Rennes, France
Last update 2016-12-28 16:22:17.33

Eric CHEVET Endoplasmic Reticulum signaling in cancer

Course and current status

From 2017: DR1 Inserm, Proteostasis and Cancer team - Inserm U1242, Université Rennes 1, Centre de lutte contre le cancer Eugène Marquis, Rennes, France

2015 - 2017: DR2 Inserm, Proteostasis and Cancer team - OSS lab, ERL440 Inserm Université Rennes 1, Centre de lutte contre le cancer Eugène Marquis, Rennes, France

2010 - 2015: Senior group leader (DR2) at INSERM, U1053, Bordeaux, France

2006 - 2010: Junior group leader (AVENIR) at INSERM, U889, Bordeaux, France

                    INSERM staff scientist (CR1)

2003 - Habilitation à Diriger la Recherche (HDR)

2001 - 2006: Assistant professor, McGill University, Montreal, Canada

1997 - 2001: post-doctoral fellow in the lab of JJM Bergeron, McGill University, Canada

1996- PhD, Molecular Biology of the Cell, Paris XI University.

Scientific summary

The "organelle, stress and cancer" team focuses on the understanding of adpatation mechanisms set in place by the normal and pathological cells to cope with their environment. The team is particularly interested in the role of the first sub-cellular compartment of the secretory pathway, the endoplasmic reticulum (ER). This compartment, which can represent up to 50% of the total cellular membranes, plays instrumental roles in the maintenance of calcium, lipides, and protein homeostasis.

When ER homeostasis is perturbed, the imbalance is sensed in the lumen of this compartment and transmitted to the cytosol and the nucleus. Three sensors have been identified thus far and named protein kinase RNA-like endoplasmic reticulum kinase (PERK), Activating Transcription Factor 6 (ATF6) and Inositol Requiring Enzyme 1 (IRE1). The signalling pathways activated downstream of these three ER stress sensors are collectively called the Unfolded Protein Response (UPR). The UPR aims at restoring ER homeostasis but if this fails, it triggers programmed cell death.

The UPR is activated in numerous pathologies including diabetes, degenerative disorders ro cancer. Our team focuses on elucidating the molecular mechanisms of ER stress in cancers (the models studied in the laboratory are glioblastoma, hepatocellular carcinoma and cholangiocarcinoma). We demonstrated that the IRE1 arm of the UPR significantly contributes to tumor growth in vitro and in vivo through the activation of its cytosolic endoribonuclease activity. The currrent projects aim at dissecting IRE1 signalling networks  in cancer and identifying natural and synthetic molecules susceptible to alter IRE1 functions. On a longer term, the experimental strategies currently developed in the laboratory will be applied to the other ER stress sensors PERK and ATF6.


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