ArticleThe Journal of biological chemistry2015
The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Loss of the HOPS complex disrupts early-to-late endosome transition, impairs endosomal recycling and induces accumulation of amphisomes.Molecular biology of the cell · 2024Article
- Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- Article
- The MyLO CRISPR-Cas9 toolkit: a markerless yeast localization and overexpression CRISPR-Cas9 toolkit.G3 (Bethesda, Md.) · 2022Article
- Article
- Small but mighty: Atg8s and Rabs in membrane dynamics during autophagy.Biochimica et biophysica acta. Molecular cell research · 2021Review
- AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering.The EMBO journal · 2020Article
- The road to lysosome-related organelles: Insights from Hermansky-Pudlak syndrome and other rare diseases.Traffic (Copenhagen, Denmark) · 2019Review
- Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.PLoS genetics · 2018Article
- Mechanism of Stx17 recruitment to autophagosomes via IRGM and mammalian Atg8 proteins.The Journal of cell biology · 2018Article
- 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
- Multivalent Rab interactions determine tether-mediated membrane fusion.Molecular biology of the cell · 2017Article
- Multiple Roles of the Small GTPase Rab7.Cells · 2016Review
- Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016Review
- Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016Review
- The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane fusion at vacuoles requires a consecutive action of the HOPS tethering complex, which is recruited by the Rab GTPase Ypt7, and vacuolar SNAREs to drive membrane fusion. It is assumed that the Sec1/Munc18-like Vps33 within the HOPS complex is largely responsible for SNARE chaperoning. Here, we present direct evidence for HOPS binding to SNAREs and the Habc domain of the Vam3 SNARE protein, which may explain its function during fusion. We show that HOPS interacts strongly with the Vam3 Habc domain, assembled Q-SNAREs, and the R-SNARE Ykt6, but not the Q-SNARE Vti1 or the Vam3 SNARE domain. Electron microscopy combined with Nanogold labeling reveals that the binding sites for vacuolar SNAREs and the Habc domain are located in the large head of the HOPS complex, where Vps16 and Vps33 have been identified before. Competition experiments suggest that HOPS bound to the Habc domain can still interact with assembled Q-SNAREs, whereas Q-SNARE binding prevents recognition of the Habc domain. In agreement, membranes carrying Vam3ΔHabc fuse poorly unless an excess of HOPS is provided. These data suggest that the Habc domain of Vam3 facilitates the assembly of the HOPS/SNARE machinery at fusion sites and thus supports efficient membrane 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.