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J. Cell Biol.,
Volume 143, Number 3, November 2, 1998 589-599
Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California, Berkeley,
California 94720
Retrograde transport from the Golgi to the
ER is an essential process. Resident ER proteins that
escape the ER and proteins that cycle between the
Golgi and the ER must be retrieved. The interdependence of anterograde and retrograde vesicle trafficking makes the dissection of both processes difficult in vivo.
We have developed an in vitro system that measures
the retrieval of a soluble reporter protein, the precursor
of the yeast pheromone 
-factor fused to a retrieval signal (HDEL) at its COOH terminus (Dean, N., and
H.R.B Pelham. 1990. J. Cell Biol. 111:369-377). Retrieval depends on the HDEL sequence; the -factor
precursor, naturally lacking this sequence, is not retrieved. A full cycle of anterograde and retrograde
transport requires a simple set of purified cytosolic proteins, including Sec18p, the Lma1p complex, Uso1p,
coatomer, and Arf1p. Among the membrane-bound
v-SNAP receptor (v-SNARE) proteins, Bos1p is required only for forward transport, Sec22p only for retrograde trafficking, and Bet1p is implicated in both avenues of transport. Putative retrograde carriers (COPI vesicles) generated from Golgi-enriched membranes
contain v-SNAREs as well as Emp47p as cargo.
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