ArticlePLoS biology2012
Sequential analysis of trans-SNARE formation in intracellular membrane fusion.
Article in PLoS biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
- Arabidopsis Qc-SNARE genes BET11 and BET12 are required for fertility and pollen tube elongation.Botanical studies · 2015Article
- Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.The Journal of biological chemistry · 2015Article
- CAPS and Munc13: CATCHRs that SNARE Vesicles.Frontiers in endocrinology · 2013Review
- Retrograde traffic from the Golgi to the endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition.Traffic (Copenhagen, Denmark) · 2013Article
- Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion.Nature communications · 2013Article
- Munc18-1 controls SNARE protein complex assembly during human sperm acrosomal exocytosis.The Journal of biological chemistry · 2012Article
- A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion.Bioarchitecture · 2012Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
SNARE complexes are required for membrane fusion in the endomembrane system. They contain coiled-coil bundles of four helices, three (Q(a), Q(b), and Q(c)) from target (t)-SNAREs and one (R) from the vesicular (v)-SNARE. NSF/Sec18 disrupts these cis-SNARE complexes, allowing reassembly of their subunits into trans-SNARE complexes and subsequent fusion. Studying these reactions in native yeast vacuoles, we found that NSF/Sec18 activates the vacuolar cis-SNARE complex by selectively displacing the vacuolar Q(a) SNARE, leaving behind a Q(bc)R subcomplex. This subcomplex serves as an acceptor for a Q(a) SNARE from the opposite membrane, leading to Q(a)-Q(bc)R trans-complexes. Activity tests of vacuoles with diagnostic distributions of inactivating mutations over the two fusion partners confirm that this distribution accounts for a major share of the fusion activity. The persistence of the Q(bc)R cis-complex and the formation of the Q(a)-Q(bc)R trans-complex are both sensitive to the Rab-GTPase inhibitor, GDI, and to mutations in the vacuolar tether complex, HOPS (HOmotypic fusion and vacuolar Protein Sorting complex). This suggests that the vacuolar Rab-GTPase, Ypt7, and HOPS restrict cis-SNARE disassembly and thereby bias trans-SNARE assembly into a preferred topology.
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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.