Aczonin, a 550-kD putative scaffolding protein of presynaptic active zones, shares homology regions with Rim and Bassoon and binds profilin
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Neurotransmitter exocytosis is restricted to the active zone, a specialized area of the presynaptic plasma membrane. We report the identification and initial characterization of aczonin, a neuron-specific 550-kD protein concentrated at the presynaptic active zone and associated with a detergent-resistant cytoskeletal subcellular fraction. Analysis of the amino acid sequences of chicken and mouse aczonin indicates an organization into multiple domains, including two pairs of Cys4 zinc fingers, a polyproline tract, and a PDZ domain and two C2 domains near the COOH terminus. The second C2 domain is subject to differential splicing. Aczonin binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. Large parts of aczonin, including the zinc finger, PDZ, and C2 domains, are homologous to Rim or to Bassoon, two other proteins concentrated in presynaptic active zones. We propose that aczonin is a scaffolding protein involved in the organization of the molecular architecture of synaptic active zones and in the orchestration of neurotransmitter vesicle trafficking.
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Piccolo and bassoon are associated with active zones in vertebrates.
“In addition to these five core active zone proteins, piccolo and bassoon (two large homologous proteins) are associated in vertebrates with active zones (tom Dieck et al., 1998; Wang et al., 1999; Fenster et al., 2000; Limbach et al., 2011), and proteins related to C. elegans SYD-1 are important for the assembly of active zones in invertebrates (Hallam et al., 2002; Patel et al., 2006; Owald et al”
From The Presynaptic Active Zone (2012) · cites this paper as Wang et al., 1999
The Abstract describes Bassoon and Piccolo as concentrated at active zones, and the Discussion says Piccolo resembles Bassoon in size and subcellular distribution. But the paper says molecular information about Piccolo was unavailable and does not establish that Piccolo and Bassoon are homologous. (LLM, conf=0.86)
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- Authors
- Wang, X., Kibschull, M., Laue, M. M., Lichte, B., Petrasch-Parwez, E., & Kilimann, M. W.
- Affiliations
- Ruhr University Bochum (DE)
- bInstitut für Anatomie, Ruhr-Universität Bochum, D-44780 Bochum, Germany
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1999-10-04
- Volume
- 147
- Issue
- 1
- Pages
- 151-162
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2164979
- OpenAlex
- W2076710726
- Cited by
- 194
- References
- 45
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 2 · 2021: 5 · 2020: 2 · 2019: 9 · 2018: 4 · 2017: 10 · 2016: 6 · 2015: 8 · 2014: 8 · 2013: 5 · 2012: 8
- FWCI
- 3.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- 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, scaffold proteins, RIM, bassoon, C2 domain, PDZ domain, zinc finger, differential splicing, neurotransmitter exocytosis, actin cytoskeleton, protein homology
- MeSH terms
- Amino Acid Sequence, Animals, Brain, Carrier Proteins, Cell Line, Cell Membrane, Chickens, Contractile Proteins, Cytoskeletal Proteins, Cytoskeleton, Humans, Microfilament Proteins, Molecular Sequence Data, Molecular Weight, Nerve Tissue Proteins, Neurons, Neuropeptides, Organ Specificity, Peptides, RNA, Messenger, Zinc Fingers, Sequence Homology, Amino Acid, Alternative Splicing, Presynaptic Terminals, GTP-Binding Proteins, Amino Acid Motifs, rab3A GTP-Binding Protein, Profilins, Mice, Rats
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