ArticleMolecular biology of the cell2008
UNC-18 promotes both the anterograde trafficking and synaptic function of syntaxin.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 75 citations in OpenAlex.
- Expression and function of Caenorhabditis elegans UNCP-18, a paralog of the SM protein UNC-18.Genetics · 2023Article
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- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
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- PXF-1 promotes synapse development at the neuromuscular junction inFrontiers in molecular neuroscience · 2022Article
- Synaptic Secretion and Beyond: Targeting Synapse and Neurotransmitters to Treat Neurodegenerative Diseases.Oxidative medicine and cellular longevity · 2022Review
- SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling.Frontiers in molecular neuroscience · 2021Review
- Open syntaxin overcomes exocytosis defects of diverse mutants in C. elegans.Nature communications · 2020Article
- Functional analysis of epilepsy-associated variants in STXBP1/Munc18-1 using humanized Caenorhabditis elegans.Epilepsia · 2020Article
- The N-peptide-binding mode is critical to Munc18-1 function in synaptic exocytosis.The Journal of biological chemistry · 2018Article
- Genetic dissection of neuropeptide cell biology at high and low activity in a defined sensory neuron.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The presynaptic machinery at the synapse of C. elegans.Invertebrate neuroscience : IN · 2018Review
- Diverse modes of synaptic signaling, regulation, and plasticity distinguish two classes ofeLife · 2017Article
- UNC-18 and Tomosyn Antagonistically Control Synaptic Vesicle Priming Downstream of UNC-13 inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Early Golgi Abnormalities and Neurodegeneration upon Loss of Presynaptic Proteins Munc18-1, Syntaxin-1, or SNAP-25.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Phosphorylation of FEZ1 by Microtubule Affinity Regulating Kinases regulates its function in presynaptic protein trafficking.Scientific reports · 2016Article
- Normal Molecular Specification and Neurodegenerative Disease-Like Death of Spinal Neurons Lacking the SNARE-Associated Synaptic Protein Munc18-1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- The trans-SNARE-regulating function of Munc18-1 is essential to synaptic exocytosis.Nature communications · 2015Article
- A pivotal role for pro-335 in balancing the dual functions of Munc18-1 domain-3a in regulated exocytosis.The Journal of biological chemistry · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The SM protein UNC-18 has been proposed to regulate several aspects of secretion, including synaptic vesicle docking, priming, and fusion. Here, we show that UNC-18 has a chaperone function in neurons, promoting anterograde transport of the plasma membrane soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein Syntaxin-1. In unc-18 mutants, UNC-64 (Caenorhabditis elegans Syntaxin-1) accumulates in neuronal cell bodies. Colocalization studies and analysis of carbohydrate modifications both suggest that this accumulation occurs in the endoplasmic reticulum. This trafficking defect is specific for UNC-64 Syntaxin-1, because 14 other SNARE proteins and two active zone markers were unaffected. UNC-18 binds to Syntaxin through at least two mechanisms: binding to closed Syntaxin, or to the N terminus of Syntaxin. It is unclear which of these binding modes mediates UNC-18 function in neurons. The chaperone function of UNC-18 was eliminated in double mutants predicted to disrupt both modes of Syntaxin binding, but it was unaffected in single mutants. By contrast, mutations predicted to disrupt UNC-18 binding to the N terminus of Syntaxin caused significant defects in locomotion behavior and responsiveness to cholinesterase inhibitors. Collectively, these results demonstrate the UNC-18 acts as a molecular chaperone for Syntaxin transport in neurons and that the two modes of UNC-18 binding to Syntaxin are involved in different aspects of UNC-18 function.
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