Formation of AP-3 transport intermediates requires Vps41 function Academic Article uri icon

Overview

MeSH Major

  • Carrier Proteins
  • Fungal Proteins
  • Membrane Proteins
  • Monomeric Clathrin Assembly Proteins
  • Nuclear Proteins
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins

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 delta-adaptin subunit, suggesting that they function together in the formation of ALP pathway transport intermediates at the late Golgi.

publication date

  • October 1999

Research

keywords

  • Academic Article

Identity

Language

  • eng

PubMed ID

  • 10559961

Additional Document Info

start page

  • 346

end page

  • 53

volume

  • 1

number

  • 6