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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Karunakaran, Vidya Wickner, William |
| Description | Author Affiliation: Karunakaran V ( From the Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, New Hamshire 03755-3844.) |
| Abstract | Vam7p, the vacuolar soluble Qc-SNARE, is essential for yeast vacuole fusion. The large tethering complex, homotypic fusion and vacuole protein sorting complex (HOPS), and phosphoinositides, which interact with the Vam7p PX domain, have each been proposed to serve as its membrane receptors. Studies with the isolated organelle cannot determine whether these receptor elements suffice and whether ligands or mutations act directly or indirectly on Vam7p binding to the membrane. Using pure components that are active in reconstituted vacuolar fusion, we now find that Vam7p binds to membranes through its combined affinities for several vacuolar membrane constituents: HOPS, phosphatidylinositol 3-phosphate, SNAREs, and acidic phospholipids. Acidic lipids allow low concentrations of Vam7p to suffice for fusion; without acidic lipids, the block to fusion is partially bypassed by high concentrations of Vam7p. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 40 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-10-04 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Membrane Metabolism Lipids Chemistry Membrane Fusion SNARE Proteins Saccharomyces Cerevisiae Proteins Synaptosomal-Associated Protein 25 Fluorescence Polarization Glutathione Multiprotein Complexes Phosphatidylinositols Protein Binding Proteolipids Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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