aying central roles in membrane integrity, cell signalling and vesicular traffic. The pathway involving inositol 1,4,5-triphosphate has been extensively characterized. IP3 derives from the hydrolysis of phosphatidylinositol 4,5-biphosphate by phospholipase C, thereby producing IP3 and DAG. IP3 acts a second messenger via its binding to the IP3R receptor on the ER membrane. The binding of IP3 to its receptor provokes the release of the ER-stored calcium into the cytoplasm, which in turn elicits a range of STA 9090 cellular responses. Calcium release from vacuoles following IP3-signalling was also observed in Saccharomyces cerevisiae. Inositol can be synthesized by intracellular processes involving conversion of glucose-6-phosphate into inositol monophosphate through a set of complex reactions of oxidation/reduction which are mediated by a unique enzyme, the inositol-1-phosphate synthase . The INO1 gene was identified in various species of yeasts, protozoa, plants and mammals. Deletion of INO1 and mutation in other genes such as IRE1 cause inositol auxotrophy in S. cerevisiae. In this yeast, expression of INO1 is under the control of IRE1 via HAC1, two key players of the UPR pathway. Schizosaccharomyces pombe is considered a good model to study the involvement of inositol in cell pathways because this yeast is naturally auxotroph for inositol due to the absence of a gene coding for an inositol-1-phosphate synthase. Studies in S. pombe have shown that absence of inositol in the culture medium is lethal for this yeast, and that partial depletion provokes sexual sterility with no effects on growth. Although S. pombe cells 1975694 die in the absence of inositol, they are able to survive longer than S. cerevisiae cells auxotroph for inositol as result of genetic manipulation . Calnexin is an ER transmembrane chaperone playing key roles in translocation, in protein folding, and in 
the quality control of newly synthesized polypeptides. Structurally, calnexin is a type I transmembrane protein of the ER containing a large lumenal domain, a transmembrane domain, and a short cytosolic tail. The lumenal domain folds into a globular structure formed by the C- and N-terminal extremities, and a hairpin structure formed by the highly conserved central domain, which is the most conserved calnexin domain across species. Calnexin interacts with client proteins via glycan-lectin or proteinprotein interactions. The knockout of calnexin in mice causes early postnatal death and severe motor disorders and is lethal in S. pombe, thus pointing to the critical cellular roles of this protein. We 17496168 showed that certain calnexin chaperone-deficient mutants are viable. Interestingly, this demonstrates that the essentiality of calnexin is not its chaperone activity but another yet to be defined cellular role. Several studies published in the recent years indicate that calnexin is involved in apoptotic processes induced by ER stresses. First indications came from a report showing that the cytosolic tail of S. pombe calnexin is required for cell death mediated by the heterologous expression of mammalian Bak, suggesting that calnexin can form a complex with lethal partners in apoptotic situations. In mammalian cells, it was shown that calnexin-deficient cells are more resistant to apoptosis. It was suggested that calnexin could act as a scaffold for the cleavage of the ER transmembrane apoptotic protein Bap31 by caspase 8 in ER-stress conditions. In addition, calnexin in mammalian cells was s