SUMMARYWe have used electron microscopy to further charac terize details of the dynamics of TGN38/41, a protein found to cycle between the ¿ram-Golgi network and the plasma membrane. Immunogold-labeling of NRK cells under steady-state conditions shows the majority of TGN38/41 is localized to the irans-most Golgi cisternae and the iraras-Golgi network. Small amounts of this mol ecule can be detected in early endosomes. Capture of cycling TGN38/41 molecules at the cell surface altered the steady state distribution. This was accomplished by binding TGN38/41 luminal domain antibodies to solid supports (beads), which were introduced to the culture media of cells. As increasing numbers of antigen-antibody complexes formed, the beads were internalized by the 'zippering mechanism' of phagocytosis. This pro vides a system that can address many questions related to the function of TGN38/41 and the trans-Golgi net work itself.