ArticleThe Journal of biological chemistry2016
The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Differential effects of lysophospholipid headgroups, acyl chain length and saturation on vacuole acidification, CaFrontiers in cell and developmental biology · 2026Article
- Broad-Spectrum Activity and Mechanisms of Action of SQ109 on a Variety of Fungi.ACS infectious diseases · 2025Article
- Use of Bio-Layer Interferometry (BLI) to Measure Binding Affinities of SNAREs and Phosphoinositides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Spectroscopic Methods for Detecting Conformational Changes During Sec18-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Assessing the Presence of Phosphoinositides on Autophagosomal Membrane in Yeast by Live Cell Imaging.Microorganisms · 2024Article
- Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020Article
- The Effects of Regulatory Lipids on Intracellular Membrane Fusion Mediated by Dynamin-Like GTPases.Frontiers in cell and developmental biology · 2020Review
- A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion.The Journal of biological chemistry · 2019Article
- Copper blocks V-ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion.Traffic (Copenhagen, Denmark) · 2019Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- The Participation of Regulatory Lipids in Vacuole Homotypic Fusion.Trends in biochemical sciences · 2019Review
- Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.The Journal of biological chemistry · 2019Article
- Phosphatidylinositol 3,5-bisphosphate regulates the transition between trans-SNARE complex formation and vacuole membrane fusion.Molecular biology of the cell · 2019Article
- Determination of Sec18-Lipid Interactions by Liposome-Binding Assay.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Real-Time Fluorescence Detection of Calcium Efflux During Vacuolar Membrane Fusion.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Traffic (Copenhagen, Denmark) · 2017Article
- Phosphatidylinositol (3,4,5)-trisphosphate binds to sortilin and competes with neurotensin: Implications for very low density lipoprotein binding.Biochemical and biophysical research communications · 2016Article
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6 authors.
Funding
Abstract
The yeast vacuole requires four SNAREs to trigger membrane fusion including the soluble Qc-SNARE Vam7. The N-terminal PX domain of Vam7 binds to the lipid phosphatidylinositol 3-phosphate (PI3P) and the tethering complex HOPS (homotypic fusion and vacuole protein sorting complex), whereas the C-terminal SNARE motif forms SNARE complexes. Vam7 also contains an uncharacterized middle domain that is predicted to be a coiled-coil domain with multiple helices. One helix contains a polybasic region (PBR) composed of Arg-164, Arg-168, Lys-172, Lys-175, Arg-179, and Lys-186. Polybasic regions are often associated with nonspecific binding to acidic phospholipids including phosphoinositides. Although the PX (phox homology) domain alone binds PI3P, we theorized that the Vam7 PBR could bind to additional acidic phospholipids enriched at fusion sites. Mutating each of the basic residues in the PBR to an alanine (Vam7-6A) led to attenuated vacuole fusion. The defective fusion of Vam7-6A was due in part to inefficient association with its cognate SNAREs and HOPS, yet the overall vacuole association of Vam7-6A was similar to wild type. Experiments testing the binding of Vam7 to specific signaling lipids showed that mutating the PBR to alanines augmented binding to PI3P. The increased binding to PI3P by Vam7-6A likely contributed to the observed wild type levels of vacuole association, whereas protein-protein interactions were diminished. PI3P binding was inhibited when the PX domain mutant Y42A was introduced into Vam7-6A to make Vam7-7A. Thus the Vam7 PBR affects PI3P binding by the PX domain and in turn affects binding to SNAREs and HOPS to support efficient fusion.
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