ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
Synaptotagmin-12 phosphorylation by cAMP-dependent protein kinase is essential for hippocampal mossy fiber LTP.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 53 citations in OpenAlex.
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- Increased vesicle fusion competence underlies long-term potentiation at hippocampal mossy fiber synapses.Science advances · 2023Article
- Mechanistic insights into cAMP-mediated presynaptic potentiation at hippocampal mossy fiber synapses.Frontiers in cellular neuroscience · 2023Review
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- cAMP-Dependent Synaptic Plasticity at the Hippocampal Mossy Fiber Terminal.Frontiers in synaptic neuroscience · 2022Review
- Potential roles of synaptotagmin family members in cancers: Recent advances and prospects.Frontiers in medicine · 2022Review
- Mammalian and Invertebrate Models as Complementary Tools for Gaining Mechanistic Insight on Muscle Responses to Spaceflight.International journal of molecular sciences · 2021Article
- Recruitment of release sites underlies chemical presynaptic potentiation at hippocampal mossy fiber boutons.PLoS biology · 2021Article
- Proteomic identification of select protein variants of the SNARE interactome associated with cognitive reserve in a large community sample.Acta neuropathologica · 2021Article
- Function of Drosophila Synaptotagmins in membrane trafficking at synapses.Cellular and molecular life sciences : CMLS · 2021Review
- Rapid CaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Differential Effect on Hippocampal Synaptic Facilitation by the Presynaptic Protein Mover.Frontiers in synaptic neuroscience · 2019Article
- SYT12 plays a critical role in oral cancer and may be a novel therapeutic target.Journal of Cancer · 2019Article
- GPCR regulation of secretion.Pharmacology & therapeutics · 2018Review
- Long-Term Plasticity of Neurotransmitter Release: Emerging Mechanisms and Contributions to Brain Function and Disease.Annual review of neuroscience · 2018Review
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Synaptotagmin-12 (Syt12) is an abundant synaptic vesicle protein that--different from other synaptic vesicle-associated synaptotagmins--does not bind Ca(2+). Syt12 is phosphorylated by cAMP-dependent protein kinase-A at serine-97 in an activity-dependent manner, suggesting a function for Syt12 in cAMP-dependent synaptic plasticity. To test this hypothesis, we here generated (1) Syt12 knock-out mice and (2) Syt12 knockin mice carrying a single amino-acid substitution [the serine-97-to-alanine- (S97A)-substitution]. Both Syt12 knock-out mice and Syt12 S97A-knockin mice were viable and fertile, and exhibited no measurable change in basal synaptic strength or short-term plasticity as analyzed in cultured cortical neurons or in acute hippocampal slices. However, both Syt12 knock-out and Syt12 S97A-knockin mice displayed a major impairment in cAMP-dependent mossy-fiber long-term potentiation (LTP) in the CA3 region of the hippocampus. This impairment was observed using different experimental configurations for inducing and monitoring mossy-fiber LTP. Moreover, although the Syt12 knock-out had no effect on the short-term potentiation of synaptic transmission induced by the adenylate-cyclase activator forskolin in cultured cortical neurons and in the CA1 region of the hippocampus, both the Syt12 knock-out and the Syt12 S97A-knockin impaired the long-term increase in mossy-fiber synaptic transmission induced by forskolin. Thus, Syt12 is essential for cAMP-dependent presynaptic LTP at mossy-fiber synapses, and a single amino-acid substitution that blocks the cAMP-dependent phosphorylation of Syt12 is sufficient to impair the function of Syt12 in mossy-fiber LTP, suggesting that cAMP-dependent phosphorylation of Syt12 on serine-97 contributes to the induction of mossy-fiber LTP.
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