Cited by 213Cellular transport and secretionNeuroscience and Neuropharmacology ResearchProtein Kinase Regulation and GTPase Signaling

A minimal domain responsible for Munc13 activity

Basu, Jayeeta, Shen, Nan, Dulubova, Irina, Lu, Jun, Guan, Rong, Guryev, Oleg, Grishin, Nick V, Rosenmund, Christian +1 more·2005·Nature Structural & Molecular Biology

Abstract

Munc13 proteins are essential in neurotransmitter release, controlling the priming of synaptic vesicles to a release-ready state. The sequences responsible for this priming activity are unknown. Here we identify a large alpha-helical domain of mammalian Munc13-1 that is autonomously folded and is sufficient to rescue the total arrest in neurotransmitter release observed in hippocampal neurons lacking Munc13s.

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Crossref · 10.1038/nsmb1001

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  • Munc13s execute their priming function via the MUN domain.

    “Munc13s execute their priming function via the MUN domain (Basu et al., 2005; Stevens et al., 2005).”

    From The Presynaptic Active Zone (2012) · cites this paper as Basu et al., 2005

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References 13 · Cited by 213

Authors
Basu, J., Shen, N., Dulubova, I., Lu, J., Guan, R., Guryev, O., Grishin, N. V., Rosenmund, C., & Rizo, J.
Affiliations
  • Baylor College of Medicine (US)
  • The University of Texas Southwestern Medical Center (US)
  • Howard Hughes Medical Institute (US)
Corresponding author
Rizo, Josep
Venue
Nature Structural & Molecular Biology
Published
2005-10-09
Volume
12
Issue
11
Pages
1017-1018
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2006528183
Cited by
213
References
13
Citations by year
2026: 3 · 2025: 9 · 2024: 4 · 2023: 9 · 2022: 16 · 2021: 8 · 2020: 3 · 2019: 8 · 2018: 10 · 2017: 22 · 2016: 10 · 2015: 7 · 2014: 9 · 2013: 9 · 2012: 9
FWCI
5.96
Type
journal article
Language
en
Open access
closed
Locations
  • Nature Structural & Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Muscular Dystrophy Association
  • National Institutes of Health
  • National Institute of Neurological Disorders and Stroke (NS51262, NS 37200, R01NS037200, R01NS051262)
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 › Protein Kinase Regulation and GTPase Signaling
Keywords
Munc13-1, Munc13, neurotransmitter release, synaptic vesicle priming, alpha-helical domain, protein domains, hippocampal neurons, synaptic vesicle exocytosis
MeSH terms
Animals, Chromatography, Gel, Exocytosis, Hippocampus, Nerve Tissue Proteins, Neurons, Structure-Activity Relationship, Sucrose, Gene Expression, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Mice, Knockout, Neurotransmitter Agents, Computational Biology, Excitatory Postsynaptic Potentials, Nuclear Magnetic Resonance, Biomolecular, Mice, Rats

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