ArticleMolecular biology of the cell2005
Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum.
Article in Molecular biology of the cell, 2005. 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, 33 citations in OpenAlex.
- Visualization of ER-to-Golgi trafficking of procollagen X.Cell structure and function · 2024Article
- SNARE chaperone Sly1 directly mediates close-range vesicle tethering.The Journal of cell biology · 2024Article
- Acetylation of SCFD1 regulates SNARE complex formation and autophagosome-lysosome fusion.Autophagy · 2023Article
- Genome-Wide Gene-Set Analysis Approaches in Amyotrophic Lateral Sclerosis.Journal of personalized medicine · 2022Review
- 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
- 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
- mTOR-mediated phosphorylation of VAMP8 and SCFD1 regulates autophagosome maturation.Nature communications · 2021Article
- Article
- Review
- Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016Review
- Remodeling of secretory compartments creates CUPS during nutrient starvation.The Journal of cell biology · 2014Article
- ER-associated retrograde SNAREs and the Dsl1 complex mediate an alternative, Sey1p-independent homotypic ER fusion pathway.Molecular biology of the cell · 2014Article
- SLY1 and Syntaxin 18 specify a distinct pathway for procollagen VII export from the endoplasmic reticulum.eLife · 2014Article
- Structural basis of Vps33A recruitment to the human HOPS complex by Vps16.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The role of Munc18-1 and its orthologs in modulation of cortical F-actin in chromaffin cells.Journal of molecular neuroscience : MN · 2012Review
- Organization of SNAREs within the Golgi stack.Cold Spring Harbor perspectives in biology · 2011Review
- Yeast Sec1p functions before and after vesicle docking.Molecular biology of the cell · 2009Article
- Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing.The EMBO journal · 2009Article
- Yarrowia lipolytica vesicle-mediated protein transport pathways.BMC evolutionary biology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sec1p/Munc18 (SM) proteins are essential for membrane fusion events in eukaryotic cells. Here we describe a systematic, structure-based mutational analysis of the yeast SM protein Sly1p, which was previously shown to function in anterograde endoplasmic reticulum (ER)-to-Golgi and intra-Golgi protein transport. Five new temperature-sensitive (ts) mutants, each carrying a single amino acid substitution in Sly1p, were identified. Unexpectedly, not all of the ts mutants exhibited striking anterograde ER-to-Golgi transport defects. For example, in cells of the novel sly1-5 mutant, transport of newly synthesized lysosomal and secreted proteins was still efficient, but the ER-resident Kar2p/BiP was missorted to the outside of the cell, and two proteins, Sed5p and Rer1p, which normally shuttle between the Golgi and the ER, failed to relocate to the ER. We also discovered that in vivo, Sly1p was associated with a SNARE complex formed on the ER, and that in vitro, the SM protein directly interacted with the ER-localized nonsyntaxin SNAREs Use1p/Slt1p and Sec20p. Furthermore, several conditional mutants defective in Golgi-to-ER transport were synthetically lethal with sly1-5. Together, these results indicate a previously unrecognized function of Sly1p in retrograde transport to the endoplasmic reticulum.
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