Assembly of the presynaptic active zone
Open accessAbstract
In a presynaptic nerve terminal, the active zone is composed of sophisticated protein machinery that enables secretion on a submillisecond time scale and precisely targets it toward postsynaptic receptors. The past two decades have provided deep insight into the roles of active zone proteins in exocytosis, but we are only beginning to understand how a neuron assembles active zone protein complexes into effective molecular machines. In this review, we outline the fundamental processes that are necessary for active zone assembly and discuss recent advances in understanding assembly mechanisms that arise from genetic, morphological and biochemical studies. We further outline the challenges ahead for understanding this important problem.
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Biophysical studies often delineate different vesicle pools at presynaptic active zones, but how these pools correlate to vesicle populations in electron micrographs or tomograms remains unclear.
“Finally, biophysical studies often delineate different vesicle pools at presynaptic active zones (AZs), specialized sites of synaptic vesicles fusion and neurotransmitter release [9–13] but how these pools correlate to vesicle populations in electron micrographs or tomograms remains unclear.”
From Presynaptic cAMP-PKA-mediated potentiation induces reconfiguration of synaptic vesicle pools and channel-vesicle coupling at hippocampal mossy fiber boutons (2024) · cites this paper as [13]
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Specific presynaptic functions require distinct Drosophila Cav2 splice isoformsPreprint
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Self-citationThe intracellular C-terminus confers compartment-specific targeting of voltage-gated Ca 2+ channelsPreprint
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Specific presynaptic functions require distinct Drosophila Cav2 splice isoformsPreprint
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Author response: Specific presynaptic functions require distinct Drosophila Cav2 splice isoforms
Bell, C., Kilo, L., Gottschalk, D., Kern, H., Arian, J., Deneke, L., Kobler, O., Rickert, C., Strauß, J., Heine, M., et al. (2024) · eLife · doi:10.7554/elife.100394.1.sa0
eLife Assessment: Specific presynaptic functions require distinct Drosophila Cav2 splice isoforms
Dickman, D. K. (2024) · eLife · doi:10.7554/elife.100394.1.sa4
Specific presynaptic functions require distinct Drosophila Cav2 splice isoformsPreprint
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PcloC ‐Mediated Phase Separation in Short‐Distance Vesicle Transport
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Self-citationAxonal dopamine release: Molecular mechanisms
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Synaptic active zones are ordered nanostructures designed by supramolecular block copolymersPreprint
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The Role of Presynaptic Cytomatrix Protein Bassoon (BSN) in Tau Pathology and Propagation
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Ultrastructural and molecular analysis of cortico-striatal dopamine hub synapses
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- Authors
- Emperador-Melero, J., & Kaeser, P. S.
- Affiliations
- Harvard University (US)
- Corresponding author
- Kaeser, Pascal S
- Venue
- Current Opinion in Neurobiology
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 63
- Pages
- 95-103
- ISSN
- 0959-4388 (ISSN-L)
- PMC
- PMC7483790
- OpenAlex
- W3026030751
- Cited by
- 109
- References
- 71
- Citations by year
- 2026: 16 · 2025: 23 · 2024: 23 · 2023: 12 · 2022: 15 · 2021: 16 · 2020: 4
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Neurobiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health
- National Institute of Neurological Disorders and Stroke
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- active zone, active zone proteins, synaptic vesicle exocytosis, neurotransmitter release, synaptic transmission, presynaptic terminals, protein complex formation
- MeSH terms
- Exocytosis, Neurons, Proteins, Synapses, Presynaptic Terminals
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