ArticleThe Journal of biological chemistry2015
The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes.
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 34 papers.
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Who cites it
34 citing papers in PubMed, 63 citations in OpenAlex.
- Molecular choreography of vesicle trafficking: Exocyst-SNARE interplay in plant defense.Journal of advanced research · 2026Review
- The exocyst in ciliogenesis.Renal failure · 2025Review
- Munc13-4 mediates tumor immune evasion by regulating the sorting and secretion of PD-L1 via exosomes.Nature communications · 2025Article
- A tale of Rabs and the exocyst complex in ciliary trafficking and biogenesis.Frontiers in cell and developmental biology · 2025Review
- Exocyst stimulates multiple steps of exocytic SNARE complex assembly and vesicle fusion.Nature structural & molecular biology · 2025Article
- Regulation of yeast polarized exocytosis by phosphoinositide lipids.Cellular and molecular life sciences : CMLS · 2024Review
- The exocyst in context.Biochemical Society transactions · 2024Review
- Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024Review
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- The machinery of vesicle fusion.Current opinion in cell biology · 2023Review
- The exocyst complex is required for the trafficking and delivery of KCa3.1 to the basolateral membrane of polarized epithelia.American journal of physiology. Cell physiology · 2023Article
- Allosteric regulation of exocyst: Discrete activation of tethering by two spatial signals.The Journal of cell biology · 2023Article
- Functional hierarchy among different Rab27 effectors involved in secretory granule exocytosis.eLife · 2023Article
- High-resolution secretory timeline from vesicle formation at the Golgi to fusion at the plasma membrane ineLife · 2022Article
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- A mechanism for exocyst-mediated tethering via Arf6 and PIP5K1C-driven phosphoinositide conversion.Current biology : CB · 2022Article
- An active tethering mechanism controls the fate of vesicles.Nature communications · 2021Article
- Munc13 binds and recruits SNAP25 to chaperone SNARE complex assembly.FEBS letters · 2021Article
- Signalling Pinpointed to the Tip: The Complex Regulatory Network That Allows Pollen Tube Growth.Plants (Basel, Switzerland) · 2020Review
- Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1.The Journal of biological chemistry · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotic cells, membrane-bound vesicles carry cargo between intracellular compartments, to and from the cell surface, and into the extracellular environment. Many conserved families of proteins are required for properly localized vesicle fusion, including the multisubunit tethering complexes and the SNARE complexes. These protein complexes work together to promote proper vesicle fusion in intracellular trafficking pathways. However, the mechanism by which the exocyst, the exocytosis-specific multisubunit tethering complex, interacts with the exocytic SNAREs to mediate vesicle targeting and fusion is currently unknown. We have demonstrated previously that the Saccharomyces cerevisiae exocyst subunit Sec6 directly bound the plasma membrane SNARE protein Sec9 in vitro and that Sec6 inhibited the assembly of the binary Sso1-Sec9 SNARE complex. Therefore, we hypothesized that the interaction between Sec6 and Sec9 prevented the assembly of premature SNARE complexes at sites of exocytosis. To map the determinants of this interaction, we used cross-linking and mass spectrometry analyses to identify residues required for binding. Mutation of residues identified by this approach resulted in a growth defect when introduced into yeast. Contrary to our previous hypothesis, we discovered that Sec6 does not change the rate of SNARE assembly but, rather, binds both the binary Sec9-Sso1 and ternary Sec9-Sso1-Snc2 SNARE complexes. Together, these results suggest a new model in which Sec6 promotes SNARE complex assembly, similar to the role proposed for other tether subunit-SNARE interactions.
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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.