The Journal of Cell Biology, Vol 111, 45-53, Copyright © 1990 by The Rockefeller University Press

ARTICLES

Isolation of a functional vesicular intermediate that mediates ER to Golgi transport in yeast

ME Groesch, H Ruohola, R Bacon, G Rossi and S Ferro-Novick
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510-8002.

We have used an in vitro assay that reconstitutes transport from the ER to the Golgi complex in yeast to identify a functional vesicular intermediate in transit to the Golgi apparatus. Permeabilized yeast cells, which serve as the donor in this assay, release a homogeneous population of vesicles that are biochemically distinct from the donor ER fraction. The isolated vesicles, containing a post-ER/pre-Golgi form of the marker protein pro-alpha-factor, were able to bind to and fuse with exogenously added Golgi membranes. The ability to isolate fusion competent vesicles provides direct evidence that ER to Golgi membrane transport is mediated by a discrete population of vesicular carriers.
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This article has been cited by other articles:

• Schweizer, A, Ericsson, M, Bachi, T, Griffiths, G, Hauri, H. (1993). Characterization of a novel 63 kDa membrane protein. Implications for the organization of the ER-to-Golgi pathway. J. Cell Sci. 104: 671-683 [Abstract]  
• Lahtinen, U., Dahllof, B., Saraste, J. (1992). Characterization of a 58 kDa cis-Golgi protein in pancreatic exocrine cells. J. Cell Sci. 103: 321-333 [Abstract]  
• Segev, N (1991). Mediation of the attachment or fusion step in vesicular transport by the GTP-binding Ypt1 protein. Science 252: 1553-1556 [Abstract]  

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