ArticleMolecular biology of the cell2004
Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.
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Who cites it
60 citing papers in PubMed, 1 synthesis or guideline pooled it, 99 citations in OpenAlex.
- The Genotypic and Phenotypic Spectrum of GOSR2 Mutations: Clinical and Pathophysiological Insights.Journal of inherited metabolic disease · 2025Pooled it
- Intriguing role of the Golgi apparatus in astrocyte function: Implications for disorders.Neural regeneration research · 2026Article
- Siamese Twins: The Multimodular Mechanisms of Golgi Maturation and Glycan Synthesis Are Coupled at Their Core.Sub-cellular biochemistry · 2026Review
- Genetic and epidemiologic assessment of mandibular cortical indices and bone mineral density in peripubertal children: the Generation R study.Clinical oral investigations · 2025Article
- Deep proteomic profiling of the intra-Golgi trafficking intermediates.Molecular biology of the cell · 2025Article
- Acute GARP depletion disrupts vesicle transport, leading to severe defects in sorting, secretion, and O-glycosylation.bioRxiv : the preprint server for biology · 2024Article
- A look beyond the QR code of SNARE proteins.Protein science : a publication of the Protein Society · 2024Article
- The Ykt6-Snap29-Syx13 SNARE complex promotes crinophagy via secretory granule fusion with Lamp1 carrier vesicles.Scientific reports · 2024Article
- Reciprocal effects of alpha-synuclein aggregation and lysosomal homeostasis in synucleinopathy models.Translational neurodegeneration · 2023Article
- 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
- Sugary Logistics Gone Wrong: Membrane Trafficking and Congenital Disorders of Glycosylation.International journal of molecular sciences · 2020Review
- A SNARE geranylgeranyltransferase essential for the organization of the Golgi apparatus.The EMBO journal · 2020Article
- The Golgi Apparatus May Be a Potential Therapeutic Target for Apoptosis-Related Neurological Diseases.Frontiers in cell and developmental biology · 2020Review
- Golgin45-Syntaxin5 Interaction Contributes to Structural Integrity of the Golgi Stack.Scientific reports · 2019Article
- Review
- Self-association and subcellular localization of Puumala hantavirus envelope proteins.Scientific reports · 2019Article
- A Kinetic View of Membrane Traffic Pathways Can Transcend the Classical View of Golgi Compartments.Frontiers in cell and developmental biology · 2019Review
- Autophagosomal YKT6 is required for fusion with lysosomes independently of syntaxin 17.The Journal of cell biology · 2018Article
- Non-canonical role of the SNARE protein Ykt6 in autophagosome-lysosome fusion.PLoS genetics · 2018Article
- A membrane fusion protein, Ykt6, regulates epithelial cell migration via microRNA-mediated suppression of Junctional Adhesion Molecule A.Cell cycle (Georgetown, Tex.) · 2018Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genetic and biochemical evidence has established that a SNARE complex consisting of syntaxin 5 (Sed5)-mYkt6 (Ykt6)-GOS28 (Gos1)-GS15 (Sft1) is required for transport of proteins across the Golgi stack in animals (yeast). We have utilized quantitative immunogold labeling to establish the cis-trans distribution of the v-SNARE GS15 and the t-SNARE subunits GOS28 and syntaxin 5. Whereas the distribution of the t-SNARE is nearly even across the Golgi stack from the cis to the trans side, the v-SNARE GS15 is present in a gradient of increasing concentration toward the trans face of the stack. This contrasts with a second distinct SNARE complex, also required for intra-Golgi transport, consisting of syntaxin 5 (Sed5)-membrin (Bos1)-ERS24 (Sec22)-rBet1 (Bet1), whose v-(rBet1) and t-SNARE subunits (membrin and ERS24), progressively decrease in concentration toward the trans face. Transport within the stack therefore appears to utilize countercurrent gradients of two Golgi SNAREpins and may involve a mechanism akin to homotypic 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.