LMA1 Binds to Vacuoles at Sec18p (NSF), Transfers upon ATP Hydrolysis to a t-SNARE (Vam3p) Complex, and Is Released during Fusion
Copyright policy )LMA1 Binds to Vacuoles at Sec18p (NSF), Transfers upon ATP Hydrolysis to a t-SNARE (Vam3p) Complex, and Is Released during Fusion
Vacuole fusion requires Sec18p (NSF), Sec17p (alpha-SNAP), Ypt7p (GTP binding protein), Vam3p (t-SNARE), Nyv1p (v-SNARE), and LMA1 (low Mr activity 1, a heterodimer of thioredoxin and I(B)2). LMA1 requires Sec18p for saturable, high-affinity binding to vacuoles, and Sec18p "priming" ATPase requires both Sec17p and LMA1. Either the sec18-1 mutation and deletion of I(B)2, or deletion of both I(B)2 and p13 (an I(B)2 homolog) causes a striking synthetic vacuole fragmentation phenotype. Upon Sec18p ATP hydrolysis, LMA1 transfers to (and stabilizes) a Vam3p complex. LMA1 is released from vacuoles in a phosphatase-regulated reaction. This LMA1 cycle explains how priming by Sec18p is coupled to t-SNARE stabilization and to fusion.
- Dartmouth College United States
Adenosine Triphosphatases, Saccharomyces cerevisiae Proteins, Microcystins, Biochemistry, Genetics and Molecular Biology(all), Qa-SNARE Proteins, Hydrolysis, Molecular Sequence Data, Membrane Proteins, Saccharomyces cerevisiae, Phosphoproteins, Membrane Fusion, Peptides, Cyclic, Fungal Proteins, Adenosine Triphosphate, Mutation, Phosphoprotein Phosphatases, Marine Toxins, Amino Acid Sequence, Enzyme Inhibitors, Glycoproteins, Protein Binding
Adenosine Triphosphatases, Saccharomyces cerevisiae Proteins, Microcystins, Biochemistry, Genetics and Molecular Biology(all), Qa-SNARE Proteins, Hydrolysis, Molecular Sequence Data, Membrane Proteins, Saccharomyces cerevisiae, Phosphoproteins, Membrane Fusion, Peptides, Cyclic, Fungal Proteins, Adenosine Triphosphate, Mutation, Phosphoprotein Phosphatases, Marine Toxins, Amino Acid Sequence, Enzyme Inhibitors, Glycoproteins, Protein Binding
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