FUNCTIONAL CHARACTERIZATION OF UNC119 IN TRYPANOSOMA BRUCEI

Abstract

Ciliary biogenesis and assembly require transport of proteins inside the flagellum which is facilitated by protein complexes comprising of intraflagellar transport (IFT) and a recently emerged pathway lipidated intraflagellar transport (LIFT). LIFT involves transport of membrane-bound lipidated cargoes by carrier proteins such as Unc119 and/or PDE6δ and the dissociation of these lipidated cargoes from their carrier proteins is regulated by the small GTPases Arl13b and Arl3 in the cilium. Trypanosoma brucei, the causative agent of sleeping sickness, possesses a highly conserved motile flagellum and is an emerging model to study flagellum/cilium biogenesis and function. Uniquely, T. brucei contains three homologues of small GTPase Arl3 namely TbArl3A, TbArl3B and TbArl3C. TbArl13 acts as a guanine nucleotide exchange factor (GEF) for TbArl3A and TbArl3C. My PhD study is focussed on deciphering the lipidated intraflagellar transport (LIFT) pathway with emphasis on characterizing the function of carrier proteins in the early divergent T. brucei.