ArticleThe Journal of biological chemistry2013
Munc18-1 protein molecules move between membrane molecular depots distinct from vesicle docking sites.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- Seeing beyond the limit: A guide to choosing the right super-resolution microscopy technique.The Journal of biological chemistry · 2021Review
- Myosin V Regulates Spatial Localization of Different Forms of Neurotransmitter Release in Central Synapses.Frontiers in synaptic neuroscience · 2021Article
- Article
- Nanoscale Organization of Vesicle Release at Central Synapses.Trends in neurosciences · 2019Review
- Article
- Navigation through the Plasma Membrane Molecular Landscape Shapes Random Organelle Movement.Current biology : CB · 2017Article
- The Munc18-1 domain 3a hinge-loop controls syntaxin-1A nanodomain assembly and engagement with the SNARE complex during secretory vesicle priming.The Journal of cell biology · 2016Article
- Resident CAPS on dense-core vesicles docks and primes vesicles for fusion.Molecular biology of the cell · 2016Article
- A molecular toggle after exocytosis sequesters the presynaptic syntaxin1a molecules involved in prior vesicle fusion.Nature communications · 2014Article
- Intellectual disability and autism spectrum disorders: causal genes and molecular mechanisms.Neuroscience and biobehavioral reviews · 2014Review
- Differential interaction of tomosyn with syntaxin and SNAP25 depends on domains in the WD40 β-propeller core and determines its inhibitory activity.The Journal of biological chemistry · 2014Article
- Imaging large cohorts of single ion channels and their activity.Frontiers in endocrinology · 2013Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Four evolutionarily conserved proteins are required for mammalian regulated exocytosis: three SNARE proteins, syntaxin, SNAP-25, and synaptobrevin, and the SM protein, Munc18-1. Here, using single-molecule imaging, we measured the spatial distribution of large cohorts of single Munc18-1 molecules correlated with the positions of single secretory vesicles in a functionally rescued Munc18-1-null cellular model. Munc18-1 molecules were nonrandomly distributed across the plasma membrane in a manner not directed by mode of interaction with syntaxin1, with a small mean number of molecules observed to reside under membrane resident vesicles. Surprisingly, we found that the majority of vesicles in fully secretion-competent cells had no Munc18-1 associated within distances relevant to plasma membrane-vesicle SNARE interactions. Live cell imaging of Munc18-1 molecule dynamics revealed that the density of Munc18-1 molecules at the plasma membrane anticorrelated with molecular speed, with single Munc18-1 molecules displaying directed motion between membrane hotspots enriched in syntaxin1a. Our findings demonstrate that Munc18-1 molecules move between membrane depots distinct from vesicle morphological docking sites.
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Registered trials
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.