Genetic evidence for a protein-kinase-A-mediated presynaptic component in NMDA-receptor-dependent forms of long-term synaptic potentiation
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The synaptic vesicle protein Rab3A is a small GTP-binding protein that interacts with rabphilin and RIM1alpha, two presynaptic substrates of protein kinase A (PKA). Mice lacking RIM1alpha and Rab3A have a defect in PKA-dependent and NMDA receptor (NMDAR)-independent presynaptic long-term potentiation (LTP) at hippocampal mossy-fiber and cerebellar parallel-fiber synapses. In contrast, the NMDAR-dependent and PKA-independent early phase of LTP at hippocampal CA3-CA1 synapses does not require these presynaptic proteins. Here, we ask whether Rab3A and RIM1alpha participate in forms of LTP that require both PKA and NMDAR activation. We find that Rab3A is necessary for corticoamygdala LTP and late-phase LTP at CA3-CA1 synapses, two forms of LTP that require NMDAR and PKA activation. The latter form of LTP also requires RIM1alpha. These results provide genetic evidence that presynaptic proteins are required in LTP induced through the postsynaptic activation of NMDARs. Thus Rab3A and its effectors are general modules for four distinct types of PKA-dependent LTP in the brain.
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In vertebrates, RIM1α is required for all types of long-term presynaptic plasticity analyzed.
“In vertebrates, RIM1α is additionally required for all types of long-term presynaptic plasticity analyzed (Castillo et al., 2002; Huang et al., 2005; Chevaleyre et al., 2007; Fourcaudot et al., 2008; Pelkey et al., 2008; Lachamp et al., 2009).”
From The Presynaptic Active Zone (2012) · cites this paper as Huang et al., 2005
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Self-citationSpine Expansion and Stabilization Associated with Long-Term Potentiation
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Chapter 6 Regulation of hippocampus-dependent memory by cyclic AMP-dependent protein kinase
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- Authors
- Huang, Y.-Y., Zakharenko, S. S., Schoch, S., Kaeser, P. S., Janz, R., Südhof, T. C., Siegelbaum, S. A., & Kandel, E. R.
- Affiliations
- Howard Hughes Medical Institute (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2005-06-20
- Volume
- 102
- Issue
- 26
- Pages
- 9365-9370
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1166627
- OpenAlex
- W2008014936
- Cited by
- 65
- References
- 3
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 3 · 2020: 1 · 2018: 2 · 2016: 2 · 2015: 2 · 2013: 3 · 2012: 3
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Cognitive Neuroscience › Memory and Neural Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- long-term potentiation, NMDA receptor, protein kinase A, Rab3A, presynaptic proteins, CA3-CA1 synapses, late-phase LTP, hippocampus, mossy fiber synapses, synaptic vesicle proteins
- MeSH terms
- Cyclic AMP, Animals, Brain, Calcium, Electrodes, Enzyme Activation, Guanosine Triphosphate, Hippocampus, Mice, Transgenic, Models, Neurological, Protein Binding, Synapses, Synaptic Vesicles, Time Factors, Receptors, N-Methyl-D-Aspartate, Presynaptic Terminals, Long-Term Potentiation, Cyclic AMP-Dependent Protein Kinases, Mice, Knockout, GTP-Binding Proteins, rab3A GTP-Binding Protein, Mice
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