ArticleProceedings of the National Academy of Sciences of the United States of America2014
The SM protein Sly1 accelerates assembly of the ER-Golgi SNARE complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- Non-Synaptic Function and Localization of Syntaxin-Binding Protein 1 in a Mouse Model of STXBP1-Related Epileptic Encephalopathy.Annals of neurology · 2026Article
- The lactate sensor NDRG3 decelerates ER-to-Golgi transport through interaction with the long isoform of syntaxin-5.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SNARE chaperone Sly1 directly mediates close-range vesicle tethering.The Journal of cell biology · 2024Article
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
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- 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
- Vesicle trafficking and vesicle fusion: mechanisms, biological functions, and their implications for potential disease therapy.Molecular biomedicine · 2022Review
- Pathway engineering facilitates efficient protein expression in Pichia pastoris.Applied microbiology and biotechnology · 2022Review
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- Article
- An imaging-based RNA interference screen for modulators of the Rab6-mediated Golgi-to-ER pathway in mammalian cells.Frontiers in cell and developmental biology · 2022Article
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021Review
- Article
- ATG16L1 autophagy pathway regulates BAX protein levels and programmed cell death.The Journal of biological chemistry · 2020Article
- Article
- Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1.The Journal of biological chemistry · 2020Article
- KPlant physiology · 2019Article
- Review
- Phosphoproteomic insights into processes influenced by the kinase-like protein DIA1/C3orf58.PeerJ · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) and Sec1/Munc18 (SM) proteins constitute the core of an ancient vesicle fusion machine that diversified into distinct sets that now function in different trafficking steps in eukaryotic cells. Deciphering their precise mode of action has proved challenging. SM proteins are thought to act primarily through one type of SNARE protein, the syntaxins. Despite high structural similarity, however, contrasting binding modes have been found for different SM proteins and syntaxins. Whereas the secretory SM protein Munc18 binds to the ‟closed conformation" of syntaxin 1, the ER-Golgi SM protein Sly1 interacts only with the N-peptide of Sed5. Recent findings, however, indicate that SM proteins might interact simultaneously with both syntaxin regions. In search for a common mechanism, we now reinvestigated the Sly1/Sed5 interaction. We found that individual Sed5 adopts a tight closed conformation. Sly1 binds to both the closed conformation and the N-peptide of Sed5, suggesting that this is the original binding mode of SM proteins and syntaxins. In contrast to Munc18, however, Sly1 facilitates SNARE complex formation by loosening the closed conformation of Sed5.
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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.