ArticleProceedings of the National Academy of Sciences of the United States of America2000
A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 67 citations in OpenAlex.
- Celastrol directly binds with VAMP7 and RAB7 to inhibit autophagy and induce apoptosis in preadipocytes.Frontiers in pharmacology · 2023Article
- Membrane Fusion and SNAREs: Interaction with Ras Proteins.International journal of molecular sciences · 2022Review
- Article
- Cargo Release from Myosin V Requires the Convergence of Parallel Pathways that Phosphorylate and Ubiquitylate the Cargo Adaptor.Current biology : CB · 2020Article
- ESCRT-dependent protein sorting is required for the viability of yeast clathrin-mediated endocytosis mutants.Traffic (Copenhagen, Denmark) · 2020Article
- FERARI is required for Rab11-dependent endocytic recycling.Nature cell biology · 2020Article
- Steric hindrance of SNARE transmembrane domain organization impairs the hemifusion-to-fusion transition.EMBO reports · 2016Article
- Regulation of lipid droplet dynamics in Saccharomyces cerevisiae depends on the Rab7-like Ypt7p, HOPS complex and V1-ATPase.Biology open · 2015Article
- Rab proteins and the compartmentalization of the endosomal system.Cold Spring Harbor perspectives in biology · 2014Review
- The roles of monomeric GTP-binding proteins in macroautophagy in Saccharomyces cerevisiae.International journal of molecular sciences · 2014Review
- Tracking of the dynamic localization of the Rab-specific HOPS subunits reveal their distinct interaction with Ypt7 and vacuoles.Cellular logistics · 2014Article
- Review series: Rab GTPases and membrane identity: causal or inconsequential?The Journal of cell biology · 2013Review
- Article
- Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration.The Journal of biological chemistry · 2009Article
- DNA watermarks: a proof of concept.BMC molecular biology · 2008Article
- Excess vacuolar SNAREs drive lysis and Rab bypass fusion.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Reversible, cooperative reactions of yeast vacuole docking.The EMBO journal · 2006Article
- Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast.Molecular biology of the cell · 2005Article
- Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion.The EMBO journal · 2005Article
- Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles.The Journal of cell biology · 2004Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The homotypic fusion of yeast vacuoles occurs in an ordered cascade of priming, docking, and fusion. The linkage between these steps has so far remained unclear. We now report that Vam7p (the vacuolar SNAP-23/25 homolog) signals from the cis-SNARE complex to Ypt7p (the vacuolar Rab/Ypt) to initiate the docking process. After Vam7p has been released from the cis-SNARE complex by Sec18p-mediated priming, it is still required for Ypt7p-dependent docking and it needs Ypt7p to remain on the vacuole. Thus, after priming, Vam7p is released from the vacuole altogether if Ypt7p has been extracted by Gdi1p or inactivated by antibody but is not released if docking is blocked simply by vacuole dilution; it is therefore Ypt7p function, and not docking per se, that retains Vam7p. In accord with this finding, cells deleted for the gene encoding Ypt7 have normal amounts of Vam7p but have little Vam7p on their isolated vacuoles. Interaction of Vam7p and Ypt7p is further indicated by two-hybrid analysis [Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., Lockshon, D., Narayan, V., Srinivasan, M., Pochart, P., et al. (2000) Nature (London) 403, 623-627] and by the effect of Vam7p on the association of the Rab/Ypt-effector HOPS complex (homotypic fusion and vacuole protein sorting; Vam2p and Vam6p plus four vacuole protein sorting class C proteins) with Ypt7p. Vam7p provides a functional link between the priming step, which releases it from the cis-SNARE complex, and docking.
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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.