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Published online 28 July 2003. doi:10.1083/jcb.200212101
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© The Rockefeller University Press, 0021-9525/2003/8/403 $5.00
The Journal of Cell Biology, Volume 162, Number 3, 403-412

Article

The ER v-SNAREs are required for GPI-anchored protein sorting from other secretory proteins upon exit from the ER



Pierre Morsomme, Cristina Prescianotto-Baschong and Howard Riezman

Biozentrum of the University of Basel, CH-4056 Basel, Switzerland

Address correspondence to Howard Riezman, Dept. of Biochemistry, University of Geneva, Sciences II, 30 quai E. Ansermet, CH-1211 Geneva, Switzerland. Tel.: 41-22-702-6469. Fax: 41-22-702-6465. email: Howard.Riezman{at}biochem.unige.ch

Glycosylphosphatidylinositol (GPI)-anchored proteins exit the ER in distinct vesicles from other secretory proteins, and this sorting event requires the Rab GTPase Ypt1p, tethering factors Uso1p, and the conserved oligomeric Golgi complex. Here we show that proper sorting depended on the vSNAREs, Bos1p, Bet1p, and Sec22p. However, the t-SNARE Sed5p was not required for protein sorting upon ER exit. Moreover, the sorting defect observed in vitro with bos1–1 extracts was also observed in vivo and was visualized by EM. Finally, transport and maturation of the GPI-anchored protein Gas1p was specifically affected in a bos1–1 mutant at semirestrictive temperature. Therefore, we propose that v-SNAREs are part of the cargo protein sorting machinery upon exit from the ER and that a correct sorting process is necessary for proper maturation of GPI-anchored proteins.

Key Words: membrane trafficking; SNARE; protein sorting; GPI; ER to Golgi

Pierre Morsomme's current address is Unité de Biochimie Physiologique, Institut des Sciences de la Vie, University of Louvain, Croix du Sud 2-20, B-1348 Louvain-la-Neuve, Belgium.

Abbreviations used in this paper: COG, conserved oligomeric Golgi; CPY, carboxypeptidase Y; GPI, glycosylphosphatidylinositol.


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