Neurotransmitter release regulated by a MALS-liprin-α presynaptic complex
Open accessAbstract
Synapses are highly specialized intercellular junctions organized by adhesive and scaffolding molecules that align presynaptic vesicular release with postsynaptic neurotransmitter receptors. The MALS/Veli–CASK–Mint-1 complex of PDZ proteins occurs on both sides of the synapse and has the potential to link transsynaptic adhesion molecules to the cytoskeleton. In this study, we purified the MALS protein complex from brain and found liprin-α as a major component. Liprin proteins organize the presynaptic active zone and regulate neurotransmitter release. Fittingly, mutant mice lacking all three MALS isoforms died perinatally with difficulty breathing and impaired excitatory synaptic transmission. Excitatory postsynaptic currents were dramatically reduced in autaptic cultures from MALS triple knockout mice due to a presynaptic deficit in vesicle cycling. These findings are consistent with a model whereby the MALS–CASK–liprin-α complex recruits components of the synaptic release machinery to adhesive proteins of the active zone.
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CASK binds in vertebrates but not in invertebrates to α-liprins and to CASKIN.
“CASK additionally binds in vertebrates but not in invertebrates to α-liprins (Olsen et al., 2005; Wei et al., 2011) and to CASKIN (Tabuchi et al., 2002).”
From The Presynaptic Active Zone (2012) · cites this paper as Olsen et al., 2005
The Results section confirms that CASK binds liprin-α2, but the Discussion says the liprin-α–CASK interaction is likely conserved in D. melanogaster and C. elegans—the opposite of the claimed vertebrate-only distinction. Olsen et al. is cited for α-liprins in the citing sentence; CASKIN has a separate citation. Page numbers are not provided in our copy. (LLM, conf=0.88)
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- Authors
- Olsen, O., Moore, K. A., Fukata, M., Kazuta, T., Trinidad, J. C., Kauer, F. W., Streuli, M., Misawa, H., Burlingame, A. L., Nicoll, R. A., & Bredt, D. S.
- Affiliations
- University of California, San Francisco (US)
- 1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
- 4ImmunoGen, Inc., Cambridge, MA 02139
- 5Department of Neurology, Metropolitan Institute for Neuroscience, Tokyo 183-8526, Japan
- ORCID
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2005-09-26
- Volume
- 170
- Issue
- 7
- Pages
- 1127-1134
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2171538
- OpenAlex
- W2129082371
- Cited by
- 128
- References
- 31
- Citations by year
- 2026: 3 · 2025: 4 · 2023: 2 · 2022: 5 · 2021: 8 · 2020: 8 · 2019: 6 · 2018: 3 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 2 · 2013: 7 · 2012: 8
- FWCI
- 3.87
- 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)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institutes of Health
- 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 › Genetics › Genetics and Neurodevelopmental Disorders
- Keywords
- Liprin-α, CASK, neurotransmitter release, active zone, PDZ domain proteins, synaptic vesicle recycling, excitatory synaptic transmission
- MeSH terms
- Animals, Carrier Proteins, Cells, Cultured, Female, Male, Membrane Proteins, Synaptic Transmission, Neurons, Particle Size, Presynaptic Terminals, Mice, Knockout, Neurotransmitter Agents, Gene Targeting, Patch-Clamp Techniques, Two-Hybrid System Techniques, Vesicular Transport Proteins, Proteomics, Macromolecular Substances, Adaptor Proteins, Signal Transducing, Mice
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