A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain
Open accessAbstract
We identify a complex of three proteins in brain that has the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion. The three proteins are: (1) CASK, a protein related to MAGUKs (membrane-associated guanylate kinases); (2) Mint1, a putative vesicular trafficking protein; and (3) Veli1, -2, and -3, vertebrate homologs of C. elegans LIN-7. CASK, Mint1, and Velis form a tight, salt-resistant complex that can be readily isolated. CASK, Mint1, and Velis contain PDZ domains in addition to other modules. However, no PDZ domains are involved in complex formation, leaving them free to recruit cell adhesion molecules, receptors, and channels to the complex. We propose that the tripartite complex acts as a nucleation site for the assembly of proteins involved in synaptic vesicle exocytosis and synaptic junctions.
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Both CASK and its C. elegans homolog Lin-2 form a tripartite complex with Velis and Mints.
“Both CASK and its C. elegans homolog Lin-2 form a tripartite complex with two other PDZ-domain proteins called Velis (also named MALS, originally discovered in C. elegans as Lin-7) and Mints (also called Lin-10; Butz et al., 1998; Kaech et al., 1998).”
From The Presynaptic Active Zone (2012) · cites this paper as Butz et al., 1998
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- Authors
- Butz, S., Okamoto, M., & Südhof, T. C.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Südhof, Thomas C
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1998-09
- Volume
- 94
- Issue
- 6
- Pages
- 773-782
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2091738825
- Cited by
- 548
- References
- 0
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 9 · 2023: 12 · 2022: 16 · 2021: 16 · 2020: 19 · 2019: 11 · 2018: 6 · 2017: 14 · 2016: 13 · 2015: 17 · 2014: 13 · 2013: 10 · 2012: 20
- FWCI
- 13.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Mental Health (R01 MH52804, R01MH052804)
- 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
- CASK, Mint1, membrane-associated guanylate kinase, PDZ domain, synaptic vesicle exocytosis, neuronal adhesion, vesicle trafficking, brain
- MeSH terms
- Animals, Brain Chemistry, Calcium-Binding Proteins, Carrier Proteins, Cell Adhesion, Cell Membrane, Cloning, Molecular, Exocytosis, Glycoproteins, Humans, Membrane Glycoproteins, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Neurons, Neuropeptides, Nucleoside-Phosphate Kinase, Protein Binding, Synaptic Vesicles, Helminth Proteins, Synaptophysin, Caenorhabditis elegans, Sequence Homology, Amino Acid, Calcium-Calmodulin-Dependent Protein Kinases, Tumor Suppressor Proteins, Caenorhabditis elegans Proteins, Vesicular Transport Proteins, Adaptor Proteins, Signal Transducing, Synaptotagmins, Mice, Rats, Guanylate Kinases
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