ArticleThe Journal of biological chemistry2013
Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed.
- HOPS recognizes each SNARE, assembling ternaryeLife · 2020Article
- Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A short region upstream of the yeast vacuolar Qa-SNARE heptad-repeats promotes membrane fusion through enhanced SNARE complex assembly.Molecular biology of the cell · 2017Article
- Coiled-coil domain containing 109B is a HIF1α-regulated gene critical for progression of human gliomas.Journal of translational medicine · 2017Article
- Article
- Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Traffic (Copenhagen, Denmark) · 2017Article
- A cascade of multiple proteins and lipids catalyzes membrane fusion.Molecular biology of the cell · 2017Review
- Improved reconstitution of yeast vacuole fusion with physiological SNARE concentrations reveals an asymmetric Rab(GTP) requirement.Molecular biology of the cell · 2016Article
- Physiological lipid composition is vital for homotypic ER membrane fusion mediated by the dynamin-related GTPase Sey1p.Scientific reports · 2016Article
- Characterization of the novel tumor-suppressor gene CCDC67 in papillary thyroid carcinoma.Oncotarget · 2016Article
- Yeast vacuolar HOPS, regulated by its kinase, exploits affinities for acidic lipids and Rab:GTP for membrane binding and to catalyze tethering and fusion.Molecular biology of the cell · 2015Article
- Article
- Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion.Scientific reports · 2014Article
- Article
- The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes.Molecular biology of the cell · 2013Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors.
Funding
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.
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