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Originally published In Press as doi:10.1074/jbc.M000917200 on June 2, 2000

J. Biol. Chem., Vol. 275, Issue 42, 32966-32973, October 20, 2000
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Aut7p, a Soluble Autophagic Factor, Participates in Multiple Membrane Trafficking Processes*

Aster Legesse-Miller, Yuval Sagiv, Rina Glozman, and Zvulun ElazarDagger

From the Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, 76100 Israel

Aut7p, a protein recently implicated in autophagic events in the yeast Saccharomyces cerevisiae, exhibits significant homology to a mammalian protein, p16, herein termed GATE-16 (Golgi-associated ATPase Enhancer of 16 kDa), 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 endoplasmic reticulum to Golgi SNAREs, specifically with BET1 and SEC22. Aut7p interacts physically with the following two v-SNAREs: Bet1p, which is involved in endoplasmic reticulum 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.

* This work was supported in part by the Israeli Science Foundation and the Weizmann Institute Minerva Center.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Incumbent of the Shloimo and Michla Tomarin Career Development Chair of Membrane Physiology. To whom correspondence should be addressed. Tel.: 972-8-9343682; Fax: 972-8-9344112; E-mail: bmzevi@weizmann.weizmann.ac.il.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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