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Vol. 11, Issue 11, 3723-3736, November 2000
Department of Internal Medicine, Washington University School of
Medicine, St. Louis, Missouri 63110
The heterotetrameric adaptor protein complex AP-3 has been shown to
function in the sorting of proteins to the endosomal/lysosomal system.
However, the mechanism of AP-3 recruitment onto membranes is poorly
understood, and it is still uncertain whether AP-3 nucleates clathrin-coated vesicles. Using purified components, we show that AP-3
and clathrin are recruited onto protein-free liposomes and Golgi-enriched membranes by a process that requires ADP-ribosylation factor (ARF) and GTP but no other proteins or nucleotides. The efficiency of recruitment onto the two sources of membranes is comparable and independent of the composition of the liposomes. Clathrin binding occurred in a cooperative manner as a function of the
membrane concentration of AP-3. Thin-section electron microscopy of
liposomes and Golgi-enriched membranes that had been incubated with
AP-3, clathrin, and ARF·GTP showed the presence of clathrin-coated buds and vesicles. These results establish that AP-3-containing clathrin-coated vesicles form in vitro and are consistent with AP-3-dependent protein transport being mediated by clathrin-coated vesicles.
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