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Christophe Erneux

I.R.I.B.H.M., Université Libre de Bruxelles, Bâtiment C, Campus Erasme, 
808 route de Lennik, 1070 Brussels, Belgium. tel 32 02 555 4162
cerneux@ulb.ac.be
Christophe Erneux

Current position: Professor at ULB (Université Libre de Bruxelles)

Introduction:

Inositol phosphates and phosphoinositides, respectively soluble and lipidic molecules, play a fundamental role in cell regulation and membrane dynamics. Phosphatidylinositol, a membrane phospholipid, can be reversibly phosphorylated at the 3, 4 and 5 positions of myo-inositol to generate phosphoinositides (PIs) (seven are currently known in mammalian cells). Phosphoinositides play a fundamental role in cell physiology, signalling and physiopathology (Blero et al., 2007). Our interest in this metabolism of phosphoinositides started with the cloning of a series of inositol polyphosphate 5-phosphatase and Ins(1,4,5)P3 3-kinases. We have purified and cloned “type I Ins(1,4,5)P3 5-phosphatase” (Verjans et al., 1994) followed by the SH2 domain containing inositol 5-phosphatase SHIP1 and SHIP2 (Drayer et al., 1996;Pesesse et al., 1997;Pesesse et al., 2001). The preferred substrate of SHIP1/2 is PI(3,4,5)P3 and the product of the reaction is PI(3,4)P2. Both PIs are able to bind to PKB and PDK1 PH domains and to facilitate PDK1 phosphoylation of PKB in vitro. Most studies in intact cells have suggested that PI(3,4,5)P3 is more important than PI(3,4)P2 for PKB activation but this is still controversial. PI(4,5)P2 can also be a substrate of SHIP2. SHIP1/2 are very much studied due to their implication in immune response, myeloid cell survival for SHIP1 and insulin signalling, the control of obesity for SHIP2 (Clement et al., 2001;Huber et al., 1999;Liu et al., 1999) and also development (Dubois et al., 2012). In addition, SHIP1/2 implication in human cancer has been shown (see Erneux et al, 2016 for a review).
The general goal of our laboratory is to understand why phosphatases and kinases that act on inositol phosphates and phosphoinositides are critical in signalling. How these enzymes are regulated and how they participate in non enzymatic properties but rather through docking properties in another aspect of our research.
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