ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2021
Presynaptic Short-Term Plasticity Persists in the Absence of PKC Phosphorylation of Munc18-1.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Alzheimer's Pathology Enhances Excitatory Synaptic Input and Integration in VTA Dopamine Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Article
- Munc13-1 couples DAG and CaScience advances · 2026Article
- PKC-dependent enhancement of glutamate input to VTA dopamine neurons in 3xTg-AD mice.bioRxiv : the preprint server for biology · 2025Article
- CaScience advances · 2025Article
- Differential SNARE chaperoning by Munc13-1 and Munc18-1 dictates fusion pore fate at the release site.Nature communications · 2024Article
- Munc13- and SNAP25-dependent molecular bridges play a key role in synaptic vesicle priming.Science advances · 2023Article
- cAMP-EPAC-PKCε-RIM1α signaling regulates presynaptic long-term potentiation and motor learning.eLife · 2023Article
- Phorbolester-activated Munc13-1 and ubMunc13-2 exert opposing effects on dense-core vesicle secretion.eLife · 2022Article
- Mechanisms of Synaptic Vesicle Exo- and Endocytosis.Biomedicines · 2022Review
- Stable and Flexible Synaptic Transmission Controlled by the Active Zone Protein Interactions.International journal of molecular sciences · 2021Review
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Post-tetanic potentiation (PTP) is a form of short-term plasticity that lasts for tens of seconds following a burst of presynaptic activity. It has been proposed that PTP arises from protein kinase C (PKC) phosphorylation of Munc18-1, an SM (Sec1/Munc-18 like) family protein that is essential for release. To test this model, we made a knock-in mouse in which all Munc18-1 PKC phosphorylation sites were eliminated through serine-to-alanine point mutations (Munc18-1SA mice), and we studied mice of either sex. The expression of Munc18-1 was not altered in Munc18-1SA mice, and there were no obvious behavioral phenotypes. At the hippocampal CA3-to-CA1 synapse and the granule cell parallel fiber (PF)-to-Purkinje cell (PC) synapse, basal transmission was largely normal except for small decreases in paired-pulse facilitation that are consistent with a slight elevation in release probability. Phorbol esters that mimic the activation of PKC by diacylglycerol still increased synaptic transmission in Munc18-1SA mice. In Munc18-1SA mice, 70% of PTP remained at CA3-to-CA1 synapses, and the amplitude of PTP was not reduced at PF-to-PC synapses. These findings indicate that at both CA3-to-CA1 and PF-to-PC synapses, phorbol esters and PTP enhance synaptic transmission primarily by mechanisms that are independent of PKC phosphorylation of Munc18-1.
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