ArticleMolecular biology of the cell2001
The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Article
- 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
- Accumulation of undegraded autophagosomes by expression of dominant-negative STX17 (syntaxin 17) mutants.Autophagy · 2017Article
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
- The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.The Journal of biological chemistry · 2015Article
- p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles.Traffic (Copenhagen, Denmark) · 2015Article
- Importance of the N-terminal domain of the Qb-SNARE Vti1p for different membrane transport steps in the yeast endosomal system.PloS one · 2013Article
- Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex.Molecular biology of the cell · 2012Article
- N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites.Molecular biology of the cell · 2011Article
- Metazoan cell biology of the HOPS tethering complex.Cellular logistics · 2011Article
- New links between vesicle coats and Rab-mediated vesicle targeting.Seminars in cell & developmental biology · 2011Review
- The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening.Nature structural & molecular biology · 2010Article
- Role of vesicle tethering factors in the ER-Golgi membrane traffic.FEBS letters · 2009Review
- SNARE function is not involved in early endosome docking.Molecular biology of the cell · 2008Article
- HOPS proofreads the trans-SNARE complex for yeast vacuole fusion.Molecular biology of the cell · 2008Article
- Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.The EMBO journal · 2005Article
- Positive and negative regulation of a SNARE protein by control of intracellular localization.Molecular biology of the cell · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homotypic fusion of yeast vacuoles requires a regulated sequence of events. During priming, Sec18p disassembles cis-SNARE complexes. The HOPS complex, which is initially associated with the cis-SNARE complex, then mediates tethering. Finally, SNAREs assemble into trans-complexes before the membranes fuse. The t-SNARE of the vacuole, Vam3p, plays a central role in the coordination of these processes. We deleted the N-terminal region of Vam3p to analyze the role of this domain in membrane fusion. The truncated protein (Vam3 Delta N) is sorted normally to the vacuole and is functional, because the vacuolar morphology is unaltered in this strain. However, in vitro vacuole fusion is strongly reduced due to the following reasons: Assembly, as well as disassembly of the cis-SNARE complex is more efficient on Vam3 Delta N vacuoles; however, the HOPS complex is not associated well with the Vam3 Delta N cis-complex. Thus, primed SNAREs from Vam3 Delta N vacuoles cannot participate efficiently in the reaction because trans-SNARE pairing is substantially reduced. We conclude that the N-terminus of Vam3p is required for coordination of priming and docking during homotypic vacuole fusion.
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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.