BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs.

G Rossi, K Kolstad, S Stone, F Palluault, S Ferro-Novick

Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.

Molecular biology of the cell 1995 Dec

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Here we report the identification of BET3, a new member of a group of interacting genes whose products have been implicated in the targeting and fusion of endoplasmic reticulum (ER) to Golgi transport vesicles with their acceptor compartment. A temperature-sensitive mutant in bet3-1 was isolated in a synthetic lethal screen designed to identify new genes whose products may interact with BET1, a type II integral membrane protein that is required for ER to Golgi transport. At 37 degrees C, bet3-1 fails to transport invertase, alpha-factor, and carboxypeptidase Y from the ER to the Golgi complex. As a consequence, this mutant accumulates dilated ER and small vesicles. The SNARE complex, a docking/fusion complex, fails to form in this mutant. Furthermore, BET3 encodes an essential 22-kDa hydrophilic protein that is conserved in evolution, which is not a component of this complex. These findings support the hypothesis that Bet3p may act before the assembly of the SNARE complex.

Citation

G Rossi, K Kolstad, S Stone, F Palluault, S Ferro-Novick. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs. Molecular biology of the cell. 1995 Dec;6(12):1769-80