Lipid droplets (LDs) are central to cellular energy homeostasis, but the pathways governing their selective degradation are not fully defined. We identify a degradation route for a specific LD subpopulation marked by the phosphatidylinositol transfer protein Pdr16. Under nutrient limitation, the Mon1–Ccz1 GEF complex, through an amphipathic helix in Ccz1, directs its Rab GTPase substrate Ypt7 to Pdr16 positive LDs, initiating their vacuolar uptake. Ypt7 activation subsequently recruits the Retromer complex to vacuole LD (vCLIP) contact sites. Crucially, we find that Retromer, likely via its cargo receptor Vps10, promotes vacuolar membrane curvature to facilitate LD invagination. However, deletion of Vps10 does not completely prevent vacuolar membrane invagination during nutrient limited conditions. We thus hypothesize that retromer functions together with its additional cargo to generate the membrane curvature surrounding LDs, thereby enabling LD degradation through vacuolar invagination. To identify potential retromer cargoes, we employed label free vacuolar proteomics (Eising et al., 2018; Gao et al., 2022), which allows comprehensive identification of vacuolar proteins for comparative analyses. We reasoned that retromer function in a mutant leads to accumulation of retromer cargo on the vacuole. To ensure data reliability, we analyzed vacuolar proteomes from wild type and vps35Δ cells during stationary phase using both Orbitrap Eclipse and timsTOF Pro mass spectrometers. We then plotted the accumulated cargoes, identified by comparing vps35Δ to wild type ratios from the Orbitrap Eclipse (x axis) and timsTOF Pro (y axis). The candidate proteins identified in this manner will be validated through co localization and co immunoprecipitation with retromer, and their roles in LD internalization will be tested.