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A fusion protein required for vesicle-mediated transport in both mammalian
cells and yeast Duncan W. Wilson*, Celeste A. Wilcox†, Gregory C. Flynn*, Ellson Chen‡, Wun-Jing Kuang‡, William J. Henzel‡, Marc R. Block†§, Axel Ullrich‡§ & James E. Rothman*
*Department of Biology, Princeton University, Princeton, New Jersey 08540, USA
†Department of Biochemistry, Stanford University, Stanford, California 94305, USA
‡Genentech Inc., 460 Point San Bruno Boulevard, South San Francisco, California 94080, USA
§Present addresses: Laboratoire de Physiologie Cellulaire, Universite Joseph Fourier, B.P. 53X, 38041 Grenoble CEDEX, France. (M.R.B.); Max-Planck Institut fur Biochemie, 8033 Martinsried, FRG (A.U.)
A protein sensitive toN-ethylmaleimide catalyses the fusion of transport vesicles with Golgi cisternae in a mammalian cell-free system. By cloning and sequencing its gene from Chinese hamster ovary cells and by use of in vitro assays, we show that this fusion protein is equivalent to the SEC18 gene product of the yeast Saccharomyces cerevisiae,known to be essential for vesicle-mediated transport from the endoplasmic reticulum to the Golgi apparatus. The mechanism of vesicular fusion is thus highly conserved, both between species and at different stages of transport.
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