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<dc:title xml:lang="fr">Rôle de l'intersectin-1 au cours du trafic membranaire : identification de nouveaux partenaires moléculaires</dc:title>
<dcterms:alternative xml:lang="en">Role of Intersectin-1 in membrane trafficking : identification of new molecular partners</dcterms:alternative>
<dc:subject xml:lang="fr">Intersectin-1</dc:subject>
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<dc:subject xml:lang="fr">Oligophrénine</dc:subject>
<dc:subject xml:lang="fr">Endocytose</dc:subject>
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<dc:subject xml:lang="en">Intersectin-1</dc:subject>
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<dc:subject xml:lang="en">Alternative splicing</dc:subject>
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<dcterms:abstract xml:lang="fr">L’homéostasie cellulaire est intimement liée au trafic membranaire, processus dynamique qui permet les échanges de lipides et de protéines entre les compartiments cellulaires mais aussi entre la cellule et le milieu extracellulaire. L’intersectin-1 (ITSN1) est une protéine d’échafaudage multifonctionnelle, impliquée dans les processus d’endocytose, d’exocytose, diverses voies de signalisation ainsi que dans la survie cellulaire. L’ensemble de mes travaux de doctorat a permis d’identifier deux nouveaux partenaires de l’ITSN1, RhoU et l’OPHN1, et de montrer leur implication dans le trafic membranaire. De plus je démontre que les variants d’épissage de l’ITSN1 pourraient avoir une spécificité d’interactiondifférente vis-à-vis de ses partenaires. Nous montrons aussi que l’ITSN1 est capable de former des complexes entre ses différentes isoformes. Ainsi, l'ensemble de ces données apportent de nouvelles connaissances sur l’interactôme d’ITSN1.</dcterms:abstract>
<dcterms:abstract xml:lang="en">The cellular homeostasis is tightly linked to the membrane trafficking, a dynamic process which allows lipid and protein exchange between the cellular compartments as well as the cell and the environment. Intersectin1 (ITSN1) is a multifunctional scaffold protein implicated in the processes of endocytosis and exocytosis, different signaling pathways and cell survival. In present study I have identified two new partners of ITSN1, RhoU and OPHN1, and demonstrated their implication in membrane trafficking. Surprisingly, I have also found that the alternative splicing of ITSN1-L can lead to the change of the specificity of its interaction with binding partners. In addition, I have shown that different ITSN1 isoforms are capable to form complexes with each other. All together these data add new knowledge to ITSN1 interactome.</dcterms:abstract>
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