ArticleEMBO reports2016
Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.
Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Simulated dynamic cholesterol redistribution favors membrane fusion pore constriction.Biophysical journal · 2023Article
- Protocol for labeling and fixation of intact lysosomes with esterified amino acid analogs to assess lysosomal expansion in living eukaryotic cells.STAR protocols · 2021Article
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Molecular mechanism of fusion pore formation driven by the neuronal SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- SNARE-mediated membrane fusion arrests at pore expansion to regulate the volume of an organelle.The EMBO journal · 2018Article
- Article
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- Regulation of Exocytotic Fusion Pores by SNARE Protein Transmembrane Domains.Frontiers in molecular neuroscience · 2017Review
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SNAREs fuse membranes in several steps. Trans-SNARE complexes juxtapose membranes, induce hemifused stalk structures, and open the fusion pore. A recent penetration model of fusion proposed that SNAREs force the hydrophilic C-termini of their transmembrane domains through the hydrophobic core of the membrane(s). In contrast, the indentation model suggests that the C-termini open the pore by locally compressing and deforming the stalk. Here we test these models in the context of yeast vacuole fusion. Addition of small hydrophilic tags renders bilayer penetration by the C-termini energetically unlikely. It preserves fusion activity, however, arguing against the penetration model. Addition of large protein tags to the C-termini permits SNARE activation, trans-SNARE pairing, and hemifusion but abolishes pore opening. Fusion proceeds if the tags are detached from the membrane by a hydrophilic spacer or if only one side of the trans-SNARE complex carries a protein tag. Thus, both sides of a trans-SNARE complex can drive pore opening. Our results are consistent with an indentation model in which multiple SNARE C-termini cooperate in opening the fusion pore by locally deforming the inner leaflets.
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