ArticleThe Journal of biological chemistry2015
Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing.
Article in The Journal of biological chemistry, 2015. 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.
- Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024Review
- Structural Roles for the Juxtamembrane Linker Region and Transmembrane Region of Synaptobrevin 2 in Membrane Fusion.Frontiers in cell and developmental biology · 2020Article
- Intracellular Vesicle Fusion Requires a Membrane-Destabilizing Peptide Located at the Juxtamembrane Region of the v-SNARE.Cell reports · 2019Article
- Synaptobrevin-2 C-Terminal Flexible Region Regulates the Discharge of Catecholamine Molecules.Biophysical journal · 2019Article
- Thermodynamically reversible paths of the first fusion intermediate reveal an important role for membrane anchors of fusion proteins.Proceedings of the National Academy of Sciences of the United States of America · 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
- v-SNARE function in chromaffin cells.Pflugers Archiv : European journal of physiology · 2018Review
- Article
- A Central Small Amino Acid in the VAMP2 Transmembrane Domain Regulates the Fusion Pore in Exocytosis.Scientific reports · 2017Article
- Fusion pores and their control of neurotransmitter and hormone release.The Journal of general physiology · 2017Review
- How and why intralumenal membrane fragments form during vacuolar lysosome fusion.Molecular biology of the cell · 2017Article
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
- Article
- Lipid-anchored Synaptobrevin Provides Little or No Support for Exocytosis or Liposome Fusion.The Journal of biological chemistry · 2016Article
- Membrane tension and membrane fusion.Current opinion in structural biology · 2015Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane fusion is induced by SNARE complexes that are anchored in both fusion partners. SNAREs zipper up from the N to C terminus bringing the two membranes into close apposition. Their transmembrane domains (TMDs) might be mere anchoring devices, deforming bilayers by mechanical force. Structural studies suggested that TMDs might also perturb lipid structure by undergoing conformational transitions or by zipping up into the bilayer. Here, we tested this latter hypothesis, which predicts that the activity of SNAREs should depend on the primary sequence of their TMDs. We replaced the TMDs of all vacuolar SNAREs (Nyv1, Vam3, and Vti1) by a lipid anchor, by a TMD from a protein unrelated to the membrane fusion machinery, or by artificial leucine-valine sequences. Individual exchange of the native SNARE TMDs against an unrelated transmembrane anchor or an artificial leucine-valine sequence yielded normal fusion activities. Fusion activity was also preserved upon pairwise exchange of the TMDs against unrelated peptides, which eliminates the possibility for specific TMD-TMD interactions. Thus, a specific primary sequence or zippering beyond the SNARE domains is not a prerequisite for fusion. Lipid-anchored Vti1 was fully active, and lipid-anchored Nyv1 permitted the reaction to proceed up to hemifusion, and lipid-anchored Vam3 interfered already before hemifusion. The unequal contribution of proteinaceous TMDs on Vam3 and Nyv1 suggests that Q- and R-SNAREs might make different contributions to the hemifusion intermediate and the opening of the fusion pore. Furthermore, our data support the view that SNARE TMDs serve as nonspecific membrane anchors in vacuole fusion.
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