Endosomal protein sorting directs the fate of many functionally important proteins. One of the essential sorting complexes involved in this process is Retromer sorting complex. This evolutionary conserved complex shepherds proteins to two different locations: the Golgi and the plasma membrane. My main interest is to understand the mechanism of retromer-mediated trafficking. In detail, using live-cell 3D imaging combined with unbiased tracking within a single cell and with high spatio-temporal resolution, my work: (1) follows the formation of vesiculo-tubular carriers mediated by retromer and associated SNX’s of different (and defined) composition emanating from the endosomal compartment and (2) determines their trafficking route(s) in cells expressing normal retromer components and subunits with mutations known to be associated with neuro-degeneration disease states. Similar as some other projects in our lab, my work is based on selective labeling of defined cellular proteins to permit identification of functional events, ultimately linking the visual observations with trafficking pathways. The approach relies on the use of gene-edited cells expressing fluorescently tagged host proteins combined with cellular visualization by high resolution real time 4D lattice light sheet microscopy (LLSM).