Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release
Open accessAbstract
We have recently isolated a novel cytomatrix at the active zone (CAZ)–associated protein, CAST, and found it directly binds another CAZ protein RIM1 and indirectly binds Munc13-1 through RIM1; RIM1 and Munc13-1 directly bind to each other and are implicated in priming of synaptic vesicles. Here, we show that all the CAZ proteins thus far known form a large molecular complex in the brain, including CAST, RIM1, Munc13-1, Bassoon, and Piccolo. RIM1 and Bassoon directly bind to the COOH terminus and central region of CAST, respectively, forming a ternary complex. Piccolo, which is structurally related to Bassoon, also binds to the Bassoon-binding region of CAST. Moreover, the microinjected RIM1- or Bassoon-binding region of CAST impairs synaptic transmission in cultured superior cervical ganglion neurons. Furthermore, the CAST-binding domain of RIM1 or Bassoon also impairs synaptic transmission in the cultured neurons. These results indicate that CAST serves as a key component of the CAZ structure and is involved in neurotransmitter release by binding these CAZ proteins.
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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 [17]
The Introduction identifies Bassoon, Piccolo, RIM1, and Munc13-1 as active-zone proteins involved in organizing its structure, and links Munc13-1 to synaptic-vesicle priming. The passages from our copy do not establish that these proteins organize the localization of voltage-gated calcium channels (searched: voltage-gated calcium channels; Ca2+ channels). (LLM, conf=0.86)
Experimental — accuracy not yet measuredRIMs and Munc13 are essential active zone proteins playing key roles in synaptic vesicle docking and priming.
“Rab3-interacting molecules (RIMs) and Munc13 are also essential active zone proteins, playing key roles in synaptic vesicle docking and priming [17].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [17]
The Introduction identifies RIM1 and Munc13-1 as active-zone proteins, and the Discussion reports that their interaction is involved in synaptic-vesicle priming (page numbers unavailable). The Introduction links vesicle docking to Rab3A, not directly to RIM1 or Munc13-1, and describes the latter proteins as implicated in priming rather than establishing that both are essential for docking and priming. (LLM, conf=0.88)
Experimental — accuracy not yet measuredBoth LTP and LTD rely on similar signal transduction cascades that regulate translation initiation.
“Both LTP and LTD rely on similar signal transduction cascades that regulate translation initiation.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [17]
The Results section on RIM1–CAST binding discusses neurotransmitter release and synaptic transmission, not translation initiation. A search of our copy for LTP, LTD, protein synthesis, and signal-transduction cascades found no passage addressing whether both forms of plasticity rely on similar cascades. (LLM, conf=0.75)
Experimental — accuracy not yet measuredThe specificity by which new proteins participate in either LTP or LTD may be determined by specific RNA-binding proteins and an activity-dependent capture mechanism.
“The specificity by which new proteins participate in either LTP or LTD may be determined by specific RNA-binding proteins and an “activity-dependent capture” mechanism.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [17]
The Introduction describes presynaptic active zones and neurotransmitter release, while the Results examine interactions among CAST, RIM1, and Bassoon; no page numbers are available in our copy. Searches for RNA-binding proteins, activity-dependent capture, and newly synthesized proteins in LTP or LTD found no passage addressing the claimed mechanism. (LLM, conf=0.76)
Experimental — accuracy not yet measuredActivation of group 1 mGluRs induces LTD that requires rapid protein synthesis within minutes.
“For instance, activation of group 1 mGluRs induces LTD that requires rapid protein synthesis within minutes.”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [17]
The Results section reports that disrupting CAST–RIM1 or CAST–Bassoon binding impairs synaptic transmission in SCG neurons; it does not address group 1 mGluR-induced LTD. Searches for mGluRs, long-term depression, and rapid protein synthesis found no passage supporting the attributed claim. Page numbers were not available in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measured
Newly synthesized proteins are thought to maintain LTP and LTD primarily through the regulation of ionotropic glutamate receptor trafficking or the stabilization of structural changes that maintain receptor density at the synapse.
“Newly synthesized proteins are thought to maintain LTP and LTD primarily through the regulation of ionotropic glutamate receptor trafficking or the stabilization of structural changes that maintain receptor density at the synapse [17].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [17]
The Introduction and Discussion address presynaptic active-zone proteins and neurotransmitter release, not how newly synthesized proteins maintain LTP or LTD. Searches for glutamate-receptor trafficking and structural changes maintaining synaptic receptor density found no passage addressing the claim; page numbers are unavailable in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredActivity-dependent capture involves a binding cascade of densin, delta-catenin, and N-cadherin, where the CaMKII/NMDAR complex serves as the initial molecular tag that captures these proteins to increase synapse size and stability.
“This activity-dependent capture involves a binding cascade of densin, delta-catenin, and N-cadherin, where the CaMKII/NMDAR complex serves as the initial molecular tag that captures these proteins to increase synapse size and stability [17,63].”
From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [17]
The Discussion (page unavailable) describes a presynaptic complex of CAST, RIM1, Munc13-1, Bassoon, and Piccolo involved in neurotransmitter release. Searches for densin, delta-catenin, N-cadherin, and a CaMKII/NMDAR molecular tag found no passage addressing the claimed activity-dependent capture or its effect on synapse size and stability. (LLM, conf=0.75)
Experimental — accuracy not yet measured
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- Ohtsuka, T., E. Takao-Rikitsu, E. Inoue, M. Inoue, M. Takeuchi, K. Matsubara, M. Deguchi-Tawarada, K. Satoh, K. Morimoto, H. Nakanishi, and Y. Takai. 2002. Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1. J. Cell Biol. 158: 577–590. 12163476 PMC2173811
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Self-citation
- Authors
- Takao-Rikitsu, E., Mochida, S., Inoue, E., Deguchi-Tawarada, M., Inoue, M., Ohtsuka, T., & Takai, Y.
- Affiliations
- 1KAN Research Institute, Kyoto 600-8815, Japan
- Tokyo Medical University (JP)
- The University of Osaka (JP)
- Corresponding author
- Ohtsuka, Toshihisa
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-01-19
- Volume
- 164
- Issue
- 2
- Pages
- 301-311
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172332
- OpenAlex
- W1964731521
- Cited by
- 221
- References
- 38
- Citations by year
- 2026: 3 · 2025: 1 · 2024: 3 · 2023: 5 · 2022: 10 · 2021: 7 · 2020: 8 · 2019: 10 · 2018: 10 · 2017: 10 · 2016: 9 · 2015: 7 · 2014: 15 · 2013: 12 · 2012: 10
- FWCI
- 6.51
- 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)
- 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 › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- CAST, RIM1, bassoon, piccolo, Munc13-1, active zone, neurotransmitter release, synaptic vesicle priming, protein-protein interaction, ternary protein complex, synaptic transmission, superior cervical ganglion neurons, cytomatrix
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Brain, Cells, Cultured, Cloning, Molecular, Cytoskeletal Proteins, Hippocampus, Kinetics, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Peptide Fragments, Proto-Oncogene Proteins, Recombinant Proteins, Synapses, Transfection, Zinc Fingers, Superior Cervical Ganglion, Neurotransmitter Agents, GTP-Binding Proteins, Adaptor Proteins, Signal Transducing, Rats
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