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Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes
A Legesse-Miller1, Y Sagiv, R Glozman
1Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, 76100 Israel.
The Journal of Biological Chemistry
|June 6, 2000
Summary
Aut7p, a yeast protein involved in autophagy, also participates in membrane trafficking. It substitutes for GATE-16 in mammalian intra-Golgi transport and interacts with key SNARE proteins.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Aut7p is a protein in yeast Saccharomyces cerevisiae linked to autophagic events.
- A homologous mammalian protein, p16, is identified as GATE-16, a Golgi-associated ATPase Enhancer.
- GATE-16 is known as a novel intra-Golgi transport factor.
Purpose of the Study:
- To investigate the involvement of Aut7p in various membrane trafficking processes.
- To determine if Aut7p can substitute for GATE-16 function in mammalian cells.
- To identify interactions of Aut7p with other proteins involved in membrane transport.
Main Methods:
- In vitro assays to assess Aut7p's substitution for GATE-16 in intra-Golgi transport.
- Genetic interaction studies with endoplasmic reticulum to Golgi SNAREs (BET1, SEC22).
- Physical interaction studies with v-SNAREs (Bet1p, Nyv1p).
Main Results:
- Aut7p largely substitutes for GATE-16 activity in mammalian intra-Golgi transport in vitro.
- Aut7p shows genetic interactions with ER to Golgi SNAREs, BET1 and SEC22.
- Aut7p physically interacts with v-SNAREs Bet1p (ER to Golgi transport) and Nyv1p (vacuolar inheritance).
Conclusions:
- Aut7p has pleiotropic effects beyond its role in autophagocytosis.
- Aut7p participates in at least two distinct membrane traffic events.
- Aut7p is a versatile protein involved in both autophagocytosis and intra-Golgi and vacuolar transport pathways.