ArticleProceedings of the National Academy of Sciences of the United States of America2009
Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 62 citations in OpenAlex.
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Broad-Spectrum Activity and Mechanisms of Action of SQ109 on a Variety of Fungi.ACS infectious diseases · 2025Article
- PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023Article
- Membrane Fusion and SNAREs: Interaction with Ras Proteins.International journal of molecular sciences · 2022Review
- The HOPS tethering complex is required to maintain signaling endosome identity and TORC1 activity.The Journal of cell biology · 2022Article
- Article
- Acetate and hypertonic stress stimulate vacuole membrane fission using distinct mechanisms.PloS one · 2022Article
- HOPS recognizes each SNARE, assembling ternaryeLife · 2020Article
- Arrest ofThe Journal of biological chemistry · 2018Article
- A cascade of multiple proteins and lipids catalyzes membrane fusion.Molecular biology of the cell · 2017Review
- Phosphatidylinositol 3-phosphates-at the interface between cell signalling and membrane traffic.The EMBO journal · 2016Review
- Physiological lipid composition is vital for homotypic ER membrane fusion mediated by the dynamin-related GTPase Sey1p.Scientific reports · 2016Article
- Phosphoinositides: Key modulators of energy metabolism.Biochimica et biophysica acta · 2015Review
- The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.The Journal of biological chemistry · 2015Article
- Vibrio effector protein VopQ inhibits fusion of V-ATPase-containing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion.Scientific reports · 2014Article
- Function and regulation of the endosomal fusion and fission machineries.Cold Spring Harbor perspectives in biology · 2014Review
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Yeast vacuole fusion requires 4 SNAREs, 2 SNARE chaperone systems (Sec17p/Sec18p/ATP and the HOPS complex), and 2 phosphoinositides, phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P(2)]. By reconstituting proteoliposomal fusion with purified components, we now show that phosphoinositides have 4 distinct roles: PI(3)P is recognized by the PX domain of the SNARE Vam7p; PI(3)P enhances the capacity of membrane-bound SNAREs to drive fusion in the absence of SNARE chaperones; either PI(3)P or PI(4,5)P(2) can activate SNARE chaperones for the recruitment of Vam7p into fusion-competent SNARE complexes; and either PI(3)P or PI(4,5)P(2) strikingly promotes synergistic SNARE complex remodeling by Sec17p/Sec18p/ATP and HOPS. This ternary synergy of phosphoinositides and 2 SNARE chaperone systems is required for rapid fusion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.