Reconstitution of retrograde transport from the Golgi to the ER in vitro. Export

@article{citeulike:3801893, abstract = {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 alpha-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 alpha-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.}, author = {Spang, A. and Schekman, R.}, citeulike-article-id = {3801893}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/9813082}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=9813082}, day = {2}, issn = {0021-9525}, journal = {The Journal of cell biology}, keywords = {budding, coatomer, copi, golgi, in\_vivo, lipids, traffic, vesicle}, month = {November}, number = {3}, pages = {589--599}, posted-at = {2008-12-17 16:47:39}, priority = {2}, title = {Reconstitution of retrograde transport from the Golgi to the ER in vitro.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/9813082}, volume = {143}, year = {1998} }

TY - JOUR ID - citeulike:3801893 L3 - citeulike-article-id:3801893 N2 - 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 alpha-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 alpha-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. IS - 3 JF - The Journal of cell biology SN - 0021-9525 EP - 599 TI - Reconstitution of retrograde transport from the Golgi to the ER in vitro. VL - 143 SP - 589 KW - budding KW - coatomer KW - copi KW - golgi KW - in_vivo KW - lipids KW - traffic KW - vesicle AU - Spang, A AU - Schekman, R PY - 1998/11/02/ UR - http://view.ncbi.nlm.nih.gov/pubmed/9813082 ER -