Cited by 908Neuroscience and Neuropharmacology ResearchCellular transport and secretionNeurobiology and Insect Physiology Research

Bruchpilot, a protein with homology to ELKS/CAST, is required for structural integrity and function of synaptic active zones in Drosophila

Open access
Wagh, Dhananjay A., Rasse, Tobias M., Asan, Esther, Hofbauer, Alois, Schwenkert, Isabell, Dürrbeck, Heike, Buchner, Sigrid, Dabauvalle, Marie-Christine +6 more·2006·Neuron

Abstract

Neurotransmitters are released at presynaptic active zones (AZs). In the fly Drosophila, monoclonal antibody (MAB) nc82 specifically labels AZs. We employ nc82 to identify Bruchpilot protein (BRP) as a previously unknown AZ component. BRP shows homology to human AZ protein ELKS/CAST/ERC, which binds RIM1 in a complex with Bassoon and Munc13-1. The C terminus of BRP displays structural similarities to multifunctional cytoskeletal proteins. During development, transcription of the bruchpilot locus (brp) coincides with neuronal differentiation. Panneural reduction of BRP expression by RNAi constructs permits a first functional characterization of this large AZ protein: larvae show reduced evoked but normal spontaneous transmission at neuromuscular junctions. In adults, we observe loss of T bars at active zones, absence of synaptic components in electroretinogram, locomotor inactivity, and unstable flight (hence "bruchpilot"-crash pilot). We propose that BRP is critical for intact AZ structure and normal-evoked neurotransmitter release at chemical synapses of Drosophila.

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Crossref · 10.1016/j.neuron.2006.02.008

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  • Drosophila expresses an ELKS fusion protein called bruchpilot that consists of an N-terminal ELKS-related domain and a C-terminal plectin-related domain.

    “In contrast to other organisms, Drosophila expresses an ELKS fusion protein called “bruchpilot” (German for “crash pilot”) that consists of an N-terminal ELKS-related domain and a C-terminal plectin-related domain (Wagh et al., 2006).”

    From The Presynaptic Active Zone (2012) · cites this paper as Wagh et al., 2006

  • Deletion of bruchpilot produces a loss of the t bars characteristic of Drosophila synapses.

    “deletion of bruchpilot produces a loss of the t bars characteristic of Drosophila synapses (Wagh et al., 2006).”

    From The Presynaptic Active Zone (2012) · cites this paper as Wagh et al., 2006

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Authors
Wagh, D. A., Rasse, T. M., Asan, E., Hofbauer, A., Schwenkert, I., Dürrbeck, H., Buchner, S., Dabauvalle, M.-C., Schmidt, M., Qin, G., Wichmann, C., Kittel, R., Sigrist, S. J., & Buchner, E.
Affiliations
  • University of Würzburg (DE)
  • European Neuroscience Institute Göttingen (DE)
  • University of Regensburg (DE)
Corresponding author
Buchner, Erich
Venue
Neuron
Publisher
Elsevier BV
Published
2006-03
Volume
49
Issue
6
Pages
833-844
ISSN
0896-6273 (ISSN-L)
OpenAlex
W2053050328
Cited by
908
References
3
Citations by year
2026: 34 · 2025: 37 · 2024: 51 · 2023: 41 · 2022: 45 · 2021: 29 · 2020: 53 · 2019: 49 · 2018: 51 · 2017: 61 · 2016: 37 · 2015: 52 · 2014: 61 · 2013: 49 · 2012: 45
FWCI
16.95
Type
journal article
Language
en
Update notices
erratum (2006-07-20)
Open access
Locations
  • Neuron (publishedVersion)
  • PubMed (publishedVersion)
  • University of Regensburg Publication Server (University of Regensburg) (acceptedVersion)
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 › Neuroscience › Cellular and Molecular Neuroscience › Neurobiology and Insect Physiology Research
Keywords
Bruchpilot, synaptic active zone, RIM1, neurotransmitter release, neuromuscular junction, T-bar, Drosophila, flight behavior, electroretinogram
MeSH terms
Animals, Behavior, Animal, Cloning, Molecular, Drosophila, Humans, Immunochemistry, Membrane Potentials, Molecular Sequence Data, Nerve Tissue Proteins, Neuromuscular Junction, RNA Polymerase I, RNA, Messenger, Blotting, Northern, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Walking, In Situ Hybridization, Presynaptic Terminals, Reverse Transcriptase Polymerase Chain Reaction, Drosophila Proteins, Animals, Genetically Modified, Dynamins, RNA, Small Interfering, Structural Homology, Protein, Microscopy, Electron, Transmission, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins

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