GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:9657146
| Citation |
Xu, Z, Sato, K and Wickner, W (1998) LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93:1125-34 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
Adenosine Triphosphatases; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Enzyme Inhibitors/pharmacology; Fungal Proteins/genetics; Fungal Proteins/metabolism; Glycoproteins/genetics; Glycoproteins/metabolism; Hydrolysis; Membrane Fusion/physiology; Membrane Proteins; Microcystins; Molecular Sequence Data; Mutation; Peptides, Cyclic/pharmacology; Phosphoprotein Phosphatases/antagonists & inhibitors; Phosphoproteins; Protein Binding; Qa-SNARE Proteins; Saccharomyces cerevisiae/cytology; Saccharomyces cerevisiae Proteins; Thioredoxins/metabolism; Vacuoles/metabolism; Vesicular Transport Proteins |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| edit table |
See also
References
See Help:References for how to manage references in GONUTS.
