Bassoon and piccolo regulate ubiquitination and link presynaptic molecular dynamics with activity-regulated gene expression
Open accessAbstract
Release of neurotransmitter is executed by complex multiprotein machinery, which is assembled around the presynaptic cytomatrix at the active zone. One well-established function of this proteinaceous scaffold is the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis, and the transmembrane molecules important for alignment of pre- and postsynaptic structures. The presynaptic cytomatrix proteins function also in processes other than the formation of a static frame for assembly of the release apparatus and synaptic vesicle cycling. They actively contribute to the regulation of multiple steps in this process and are themselves an important subject of regulation during neuronal plasticity. We are only beginning to understand the mechanisms and signalling pathways controlling these regulations. They are mainly dependent on posttranslational modifications, including phosphorylation and small-molecules conjugation, such as ubiquitination. Ubiquitination of presynaptic proteins might lead to their degradation by proteasomes, but evidence is growing that this modification also affects their function independently of their degradation. Signalling from presynapse to nucleus, which works on a much slower time scale and more globally, emerged as an important mechanism for persistent usage-dependent and homeostatic neuronal plasticity. Recently, two new functions for the largest presynaptic scaffolding proteins b…
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The presynaptic active zone contains scaffolding proteins including bassoon, piccolo, RIMs, and munc13 that organize vesicle priming and the localization of voltage-gated calcium channels.
“At the presynaptic active zone, scaffolding proteins including bassoon, piccolo, RIMs, and munc13 organize vesicle priming and the localization of voltage-gated calcium channels.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [15]
Bassoon and Piccolo roles include the assembly of active zones, the precise localization of voltage-gated Ca2+ channels near release sites, and synaptic vesicle priming.
“Their roles include the assembly of active zones, the precise localization of voltage-gated Ca2+ channels near release sites, and synaptic vesicle priming [15,16].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [15]
LTD is initiated by the dephosphorylation of TARPs by PP1, which disrupts their interaction with PSD-95 and releases GluA1 subunits.
“This process is initiated by the dephosphorylation of TARPs by PP1, which disrupts their interaction with PSD-95 and releases GluA1 subunits.15”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [15]
Subsequent dephosphorylation of GluA1 at the S845 site further promotes receptor endocytosis.
“Subsequent dephosphorylation of GluA1 at the S845 site further promotes receptor endocytosis.15”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [15]
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Li, J., Li, Y., Lin, S., Rao, J., & Zhao, H. (2026) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1014323 · Cited by 1 · see citing works
Synaptic signalling and plasticity: emerging new players
Tóth, K. (2016) · The Journal of Physiology · doi:10.1113/jp272719 · Cited by 1 · see citing works
The presynaptic-based mechanism for learning and memory
Kim, S. H. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00087-0
The Role of Presynaptic Cytomatrix Protein Bassoon (BSN) in Tau Pathology and Propagation
Oo, W. J., Sia, W. T., Lee, J. Y., Chen, C. H., Chang, W., & Chye, S. M. (2026) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273400895251129055504
L-DOPA Promotes Post-Treatment Neurovascular and Synaptic Homeostasis in Early Diabetic Retinopathy
Chlan, E., Li, C., Bales, K. L., Wood, L. B., & Pardue, M. T. (2026) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.67.8.42
- Authors
- Ivanova, D., Dirks, A., & Fejtova, A.
- Affiliations
- Leibniz Institute for Neurobiology (DE)
- RG Presynaptic Plasticity Leibniz Institute for Neurobiology Magdeburg Germany
- ORCID
- Ivanova, Daniela
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2016-04-24
- Volume
- 594
- Issue
- 19
- Pages
- 5441-5448
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- PMC
- PMC5043050
- OpenAlex
- W2284057097
- Cited by
- 37
- References
- 56
- Citations by year
- 2026: 8 · 2025: 3 · 2024: 3 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 2
- FWCI
- 0.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journal of Physiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- bassoon, piccolo, ubiquitination, proteasome-mediated proteolysis, short-term plasticity, neuroplasticity, neurotransmitter release, synaptic vesicle recycling
- MeSH terms
- Alcohol Oxidoreductases, Animals, Brain Diseases, Cytoskeletal Proteins, DNA-Binding Proteins, Gene Expression Regulation, Nerve Tissue Proteins, Neuropeptides, Synapses, Neurotransmitter Agents, Ubiquitination, Molecular Dynamics Simulation
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