This work was dedicated to the study of the AdcA protein in Dictyostelium discoideum. AdcA has been dentified through its arrestin domain. Its arrestin core is extended on both sides by several domains among which a FYVE domain and a triplicated histidinerich domain. Subcellular localization studies of the endogenous protein or tagged AdcA forms coupled to the use of various endocytic markers showed that AdcA is present on early endosomes. The study of AdcA's different sub-domains has highlighted a role of the FYVE domain in this localization and a role of the histidine-rich domain in the metal-dependent oligomerization of the protein. My experimental work using an engineered adcA null strain suggests that AdcA could be involved in the recycling pathway going from early endosomes to the plasma membrane. By the use of the yeast two hybrid screen and pull down experiments, I have shown that AdcA is able to interact with the small G protein ArfA. This result fits with a role of AdcA on recycling vesicles where the protein could, in association with ArfA, sort membrane proteins for recycling.
