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Cited by 9Neuroscience and Neuropharmacology ResearchCellular transport and secretionExtracellular vesicles in disease

Macromolecular complexes at active zones: integrated nano-machineries for neurotransmitter release

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Chua, John Jia En·2014·Cellular and Molecular Life Sciences
DOI 10.1007/s00018-014-1657-5PMC PMC11113288
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Abstract

The release of neurotransmitters from synaptic vesicles exocytosing at presynaptic nerve terminals is a critical event in the initiation of synaptic transmission. This event occurs at specialized sites known as active zones. The task of faithfully executing various steps in the process is undertaken by careful orchestration of overlapping sets of molecular nano-machineries upon a core macromolecular scaffold situated at active zones. However, their composition remains incompletely elucidated. This review provides an overview of the role of the active zone in mediating neurotransmitter release and summarizes the recent progress using neuroproteomic approaches to decipher their composition. Key proteins of these nano-machineries are highlighted.

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  • RIMs, Munc13, CAST/ELKS, and Bassoon/Piccolo form a large molecular complex in the brain, creating a central interaction node where domains of Piccolo, Bassoon, CAST, and RIM1 converge on the N-terminal of Munc13-1.

    “These proteins, along with CAST/ELKS and Bassoon/Piccolo, form a large molecular complex in the brain, creating a central interaction node where domains of Piccolo, Bassoon, CAST, and RIM1 converge on the N-terminal of Munc13-1 [18,19].”

    From Molecular Physiology of the Neuronal Synapse (2026) · cites this paper as [18]

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Cited by

Sorted by citations

  • Molecular Physiology of the Neuronal Synapse

    Ramírez-Expósito, M. J., Cueto-Ureña, C., & Martínez-Martos, J. M. (2026) · Current Issues in Molecular Biology · doi:10.3390/cimb48010088 · Cited by 6 · see citing works

    “These proteins, along with CAST/ELKS and Bassoon/Piccolo, form a large molecular complex in the brain, creating a central interaction node where domains of Piccolo, Bassoon, CAST, and RIM1 converge on the N-terminal of Munc13-1 [18,19].”

Authors
Chua, J. J. E.
Affiliations
Max Planck Society (DE)
Corresponding author
Chua, John Jia En
ORCID
Chua, John Jia En
Venue
Cellular and Molecular Life Sciences
Publisher
Springer Science and Business Media LLC
Published
2014-06-10
Volume
71
Issue
20
Pages
3903-3916
ISSN
  • 1420-682X (ISSN-L)
  • 1420-9071
DOI
10.1007/s00018-014-1657-5
PMC
PMC11113288
OpenAlex
W2018646703
Cited by
9
References
17
Citations by year
2026: 1 · 2025: 1 · 2018: 1 · 2017: 1 · 2016: 3 · 2015: 2
FWCI
0.23
Type
journal article
Language
en
Open access
Licence
www.springer.com/tdm (tdm)
Locations
  • Cellular and Molecular Life Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Digital Library (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
European Commission
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 › Extracellular vesicles in disease
Keywords
active zone, neurotransmitter release, synaptic vesicle exocytosis, presynaptic terminals, synaptic transmission, macromolecular complexes, synaptic proteins, neuroproteomics
MeSH terms
Exocytosis, Humans, Synaptic Transmission, Synaptic Vesicles, Neurotransmitter Agents, Calcium Signaling, SNARE Proteins

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