Lipids have a signaling and metabolic role in the cell of all organisms. In eukaryote organisms and in some bacteria, they are stored in a cytoplasmic specific organelle terms lipid droplet, or lipid body (LB) and can be mobilized in response of the nutritional needs of the organism. LBs are constituted of a core of neutral lipids, mainly triacylglycerols and steryl esters, surrounded by a phospholipid monolayer membrane. It is now known that LB shows a complex and dynamic proteome and makes interactions with other organelles for lipid exchange. The aim of this study was to focus on the involvement in the dynamic of S. cerevisiae LBs of a protein from the intracellular traffic, the small GTPase Rab7p homolog Ypt7p, known to be localized on vacuole and late endosome. Using LC-MS/MS proteomic analyses of purified LBs, we confirmed the association of Ypt7p with LBs. In order to visualize the relationship between the LBs and the vacuole, Epi-fluorescence microscopy of GFP-YPT7-ERG6-RFP strain was carried out. It showed a co-localization of LBs (identified by the emission of the tagged RFP sterol- 24-methyltransferase, Erg6p LB protein) and vacuole. To confirm this observation, confocal microscopy was done. It rather showed a close association between the two organelles. To identify Ypt7p as the protein involved in this association, we studied its impact on the content of fatty acids from mutant strains, ypt7 and TEF-YPT7 (overexpressor). It showed that the deletion, and mostly, the overexpression of Ypt7p, leads to the increase of the total fatty acid content. Using electron microscopy, LB morphology was effectively found modified in mutants, confirming the involvement of Ypt7p in the dynamic of LBs. Several potential Ypt7p partners were identified using co-immunoprecipitation of purified LBs. Interestingly, analysis of strains deleted in identified partners revealed a role of some on the fatty acid content, as Ypt7p did. Further validations, like FRET microscopy, will be done to confirm the interaction between Ypt7p and these proteins.