Author: ["Peter Rehling","Tamara Darsow","David J. Katzmann","Scott D. Emr"]
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Abstract
Transport of a subset of membrane proteins to the yeast vacuole requires the function of the AP-3 adaptor protein complex. To define the molecular requirements of vesicular transport in this pathway, we used a biochemical approach to analyse the formation and content of the AP-3 transport intermediate. A vam3tsf (vacuolar t-SNARE) mutant blocks vesicle docking and fusion with the vacuole and causes the accumulation of 50–130-nanometre membrane vesicles, which we isolated and showed by biochemical analysis and immunocytochemistry to contain both AP-3 adaptors and alkaline phosphatase (ALP) pathway cargoes. Inactivation of AP-3 or the protein Vps41 blocks formation of this vesicular intermediate. Vps41 binds to the AP-3 δ-adaptin subunit, suggesting that they function together in the formation of ALP pathway transport intermediates at the late Golgi.Cite this article
Rehling, P., Darsow, T., Katzmann, D. et al. Formation of AP-3 transport intermediates requires Vps41 function. Nat Cell Biol 1, 346–353 (1999). https://doi.org/10.1038/14037 