ArticleMolecular biology of the cell2004
Positive and negative regulation of a SNARE protein by control of intracellular localization.
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 98 papers.
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Who cites it
98 citing papers in PubMed.
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- Tom70-mediated mitochondria-nuclear envelope contacts regulate nuclear pore complex inheritance during gametogenesis.bioRxiv : the preprint server for biology · 2025Article
- PILS-Nir1 is a sensitive phosphatidic acid biosensor that reveals mechanisms of lipid production.The Journal of cell biology · 2025Article
- Nir2 crystal structures reveal a phosphatidic acid-sensing mechanism at ER-PM contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- PILS-Nir1 is a novel phosphatidic acid biosensor that reveals mechanisms of lipid production.bioRxiv : the preprint server for biology · 2025Article
- Pex30-dependent membrane contact sites maintain ER lipid homeostasis.The Journal of cell biology · 2025Article
- Phosphatidic acid signaling in modulating plant reproduction and architecture.Plant communications · 2025Review
- SNARE mimicry by the CD225 domain of IFITM3 enables regulation of homotypic late endosome fusion.bioRxiv : the preprint server for biology · 2024Article
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024Review
- Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024Review
- Meiosis II spindle disassembly requires two distinct pathways.Molecular biology of the cell · 2023Article
- Recruitment of the lipid kinase Mss4 to the meiotic spindle pole promotes prospore membrane formation inMolecular biology of the cell · 2023Article
- When Phosphatases Go Mad: The Molecular Basis for Toxicity of Yeast Ppz1.International journal of molecular sciences · 2022Review
- Programmed cortical ER collapse drives selective ER degradation and inheritance in yeast meiosis.The Journal of cell biology · 2021Article
- Suppression of Vps13 adaptor protein mutants reveals a central role for PI4P in regulating prospore membrane extension.PLoS genetics · 2021Article
- Genetic Dissection of Vps13 Regulation in Yeast Using Disease Mutations from Human Orthologs.International journal of molecular sciences · 2021Article
- The Smk1 MAPK and Its Activator, Ssp2, Are Required for Late Prospore Membrane Development in SporulatingJournal of fungi (Basel, Switzerland) · 2021Article
- A Noncanonical Hippo Pathway Regulates Spindle Disassembly and Cytokinesis During Meiosis inGenetics · 2020Article
38 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
In Saccharomyces cerevisiae, the developmentally regulated Soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) protein Spo20p mediates the fusion of vesicles with the prospore membrane, which is required for the formation of spores. Spo20p is subject to both positive and negative regulation by separate sequences in its aminoterminal domain. We report that the positive activity is conferred by a short, amphipathic helix that is sufficient to confer plasma membrane or prospore membrane localization to green fluorescent protein. In vitro, this helix binds to acidic phospholipids, and mutations that reduce or eliminate phospholipid binding in vitro inactivate Spo20p in vivo. Genetic manipulation of phospholipid pools indicates that the likely in vivo ligand of this domain is phosphatidic acid. The inhibitory activity is a nuclear targeting signal, which confers nuclear localization in vegetative cells and in cells entering meiosis. However, as cells initiate spore formation, fusions containing the inhibitory domain exit the nucleus and localize to the nascent prospore membrane. Thus, the SNARE Spo20p is both positively and negatively regulated by control of its intracellular localization.
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