Aut7p, a Soluble Autophagic Factor, Participates in Multiple Membrane Trafficking Processes*
Abstract
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 ATPaseEnhancer 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 withBET1 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.
- ER
- endoplasmic reticulum
- NSF
- N-ethylmaleimide-sensitive fusion protein
- SNAP
- NSF-attachment protein
- SNARE
- SNAP receptor
- CPY
- carboxypeptidase Y
- Cvt
- cytoplasm to vacuole targeting
- PCR
- polymerase chain reaction
- PAGE
- polyacrylamide gel electrophoresis
- WT
- wild type
- Received February 4, 2000.
- Revision received May 11, 2000.
- The American Society for Biochemistry and Molecular Biology, Inc.











