Identification of an elaborate complex mediating postsynaptic inhibition
Open accessAbstract
Inhibitory synapses dampen neuronal activity through postsynaptic hyperpolarization. The composition of the inhibitory postsynapse and the mechanistic basis of its regulation, however, remain poorly understood. We used an in vivo chemico-genetic proximity-labeling approach to discover inhibitory postsynaptic proteins. Quantitative mass spectrometry not only recapitulated known inhibitory postsynaptic proteins but also revealed a large network of new proteins, many of which are either implicated in neurodevelopmental disorders or are of unknown function. Clustered regularly interspaced short palindromic repeats (CRISPR) depletion of one of these previously uncharacterized proteins, InSyn1, led to decreased postsynaptic inhibitory sites, reduced the frequency of miniature inhibitory currents, and increased excitability in the hippocampus. Our findings uncover a rich and functionally diverse assemblage of previously unknown proteins that regulate postsynaptic inhibition and might contribute to developmental brain disorders.
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By fusing BirA* to a bait protein with a synaptic localization signal or nuclear pore signal, BirA* expression was specifically guided to the synapse or nuclear pore complex to achieve biotinylation of the respective proteomes.
“By fusing BirA* to a bait protein with a synaptic localization signal or nuclear pore signal, BirA* expression was specifically guided to the synapse or nuclear pore complex to achieve biotinylation of the respective proteomes [167, 168].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [168]
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- Authors
- Uezu, A., Kanak, D. J., Bradshaw, T. W. A., Soderblom, E. J., Catavero, C. M., Burette, A. C., Weinberg, R. J., & Soderling, S. H.
- Affiliations
- Duke University (US)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Kanak, Daniel J.
- Bradshaw, Tyler W. A.
- Soderling, Scott H.
- ORCID
- Venue
- Science
- Published
- 2016-09-09
- Volume
- 353
- Issue
- 6304
- Pages
- 1123-1129
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5432043
- OpenAlex
- W2512022815
- Cited by
- 354
- References
- 61
- Citations by year
- 2026: 26 · 2025: 45 · 2024: 55 · 2023: 38 · 2022: 40 · 2021: 37 · 2020: 36 · 2019: 28 · 2018: 32 · 2017: 16 · 2016: 1
- FWCI
- 14.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- NIH (MH104736, NS039444)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- postsynaptic inhibition, inhibitory synapses, hippocampal excitability, neurodevelopmental disorders
- MeSH terms
- Animals, Brain Diseases, Carrier Proteins, Hippocampus, Membrane Proteins, Mice, Inbred C57BL, Mutation, Nerve Tissue Proteins, Neural Inhibition, Mass Spectrometry, Proteome, Mice, Post-Synaptic Density, Clustered Regularly Interspaced Short Palindromic Repeats
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