Formation of AP-3 transport intermediates requires Vps41 function

Peter Rehling, Tamara Darsow, David J. Katzmann, Scott D. Emr

Research output: Contribution to journalArticlepeer-review

96 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)346-353
Number of pages8
JournalNature Cell Biology
Issue number6
StatePublished - Oct 1999

ASJC Scopus subject areas

  • Cell Biology


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