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Papers In Press, published online ahead of print June 2, 2000
Dept. of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100
Corresponding Author: bmzevi{at}wicc.weizmann.ac.il
Aut7p, a protein recently implicated in autophagic events in the yeast Saccharomyces cerevisiae, exhibits significant homology to a mammalian protein, p16 (herein termed Golgi-associated ATPase Enhancer of 16 kD (GATE-16), a novel intra-Golgi transport factor. Here we provide evidence for the involvement of Aut7p in different membrane trafficking processes. Aut7p largely substitutes for the activity of GATE-16 in mammalian intra-Golgi transport in vitro. In vivo, AUT7 interacts genetically with ER-to-Golgi SNAREs, specifically with BET1 and SEC22. Aut7p interacts physically with two v-SNAREs: Bet1p, which is involved in ER-to-Golgi vesicular transport, and Nyv1p, implicated in vacuolar inheritance. We suggest that, in addition to its role in autophagocytosis, Aut7p has pleiotropic effects, and participates in at least two membrane traffic events.
J. Biol. Chem, 10.1074/jbc.M000917200
Submitted on February 4, 2000
Revised on May 11, 2000
Accepted on June 2, 2000
Aut7p, a Soluble Autophagic Factor, Participates in Multiple Membrane Trafficking Processes
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