ArticleProceedings of the National Academy of Sciences of the United States of America2009
The N-terminal peptide of the syntaxin Tlg2p modulates binding of its closed conformation to Vps45p.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Article
- VPS45 is required for both diffuse and tip growth ofFrontiers in plant science · 2023Article
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- Dual Sites for SEC11 on the SNARE SYP121 Implicate a Binding Exchange during Secretory Traffic.Plant physiology · 2019Article
- The N-peptide-binding mode is critical to Munc18-1 function in synaptic exocytosis.The Journal of biological chemistry · 2018Article
- Evidence for a conserved inhibitory binding mode between the membrane fusion assembly factors Munc18 and syntaxin in animals.The Journal of biological chemistry · 2017Article
- Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016Review
- Binding of SEC11 indicates its role in SNARE recycling after vesicle fusion and identifies two pathways for vesicular traffic to the plasma membrane.The Plant cell · 2015Article
- The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.The Journal of biological chemistry · 2015Article
- Loss of the Sec1/Munc18-family proteins VPS-33.2 and VPS-33.1 bypasses a block in endosome maturation in Caenorhabditis elegans.Molecular biology of the cell · 2014Article
- The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Comparative studies of Munc18c and Munc18-1 reveal conserved and divergent mechanisms of Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Functional separation of endosomal fusion factors and the class C core vacuole/endosome tethering (CORVET) complex in endosome biogenesis.The Journal of biological chemistry · 2013Article
- Review
- A genome-wide screening of potential target genes to enhance the antifungal activity of micafungin in Schizosaccharomyces pombe.PloS one · 2013Article
- Article
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Authors and funding
6 authors.
Funding
Abstract
The Sec1/Munc18 (SM) protein family regulates intracellular trafficking through interactions with individual SNARE proteins and assembled SNARE complexes. Revealing a common mechanism of this regulation has been challenging, largely because of the multiple modes of interaction observed between SM proteins and their cognate syntaxin-type SNAREs. These modes include binding of the SM to a closed conformation of syntaxin, binding to the N-terminal peptide of syntaxin, binding to assembled SNARE complexes, and/or binding to nonsyntaxin SNAREs. The SM protein Vps45p, which regulates endosomal trafficking in yeast, binds the conserved N-terminal peptide of the syntaxin Tlg2p. We used size exclusion chromatography and a quantitative fluorescent gel mobility shift assay to reveal an additional binding site that does not require the Tlg2p N-peptide. Characterization of Tlg2p mutants and truncations indicate that this binding site corresponds to a closed conformation of Tlg2p. Furthermore, the Tlg2p N-peptide competes with the closed conformation for binding, suggesting a fundamental regulatory mechanism for SM-syntaxin interactions in SNARE assembly and membrane fusion.
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