The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Control of neuronal synapse specification by a highly dedicated alternative splicing program
Abstract
Synapse identity through specific splicing: What are the mechanisms that create different, highly specific types of synapses? Traunmüller et al. found that the RNA-binding protein SLM2 regulated a very small number of alternative splicing decisions in mouse hippocampal neurons. Disrupting this splicing program resulted in specific defects in transsynaptic protein complexes. Glutamatergic transmission and synaptic plasticity were impaired. Genetically restoring one single alternative splicing event was enough to recover synaptic plasticity. SLM2 thus activates a highly specific alternative splicing program that controls the properties of glutamatergic synapses. Science , this issue p. 982
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“The regulation of NRXN1 splicing, including the formation of aberrant splice sites by specific RBPs, is poorly understood; >100 RBPs are predicted to interact with NRXN1 mRNA in a cell-type42,43 and neuronal activity23 dependent-manner.”
From Phenotypic complexities of rare heterozygous neurexin-1 deletions (2025) · cites this paper as [23]
In the citing paper
“For example, KH-domain STAR-family RBPs regulate SS4+ in a neuronal activity dependent manner23–25, mediating trans-synaptic signaling by varying interactions among a host of post-synaptic ligands.”
From Phenotypic complexities of rare heterozygous neurexin-1 deletions (2025) · cites this paper as [23]
Citations
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Self-citationSAM68 Regulates Neuronal Activity-Dependent Alternative Splicing of Neurexin-1
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Self-citationEssential roles for the splicing regulator nSR100/SRRM4 during nervous system development
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Neuronal cell type–specific alternative splicing is regulated by the KH domain protein SLM1
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Cited by
Synaptic Neurexin Complexes: A Molecular Code for the Logic of Neural Circuits
Südhof, T. C. (2017) · Cell · doi:10.1016/j.cell.2017.10.024 · Cited by 810
A cross-species proteomic map reveals neoteny of human synapse development
Wang, L., Pang, K., Zhou, L., Cebrián-Silla, A., González-Granero, S., Wang, S., Bi, Q., White, M. L., Ho, B., Li, J., et al. (2023) · Nature · doi:10.1038/s41586-023-06542-2 · Cited by 82
A cross-species proteomic map reveals neoteny of human synapse development
Wang, L., Pang, K., Zhou, L., Cebrián-Silla, A., González-Granero, S., Wang, S., Bi, Q., White, M. L., Ho, B., Li, J., et al. (2022) · doi:10.1101/2022.10.24.513541 · Cited by 82
Phenotypic complexities of rare heterozygous neurexin-1 deletions
Fernando, M. B., Fan, Y., Zhang, Y., Tokolyi, A., Murphy, A. N., Kammourh, S., Deans, P. J. M., Ghorbani, S., Onatzevitch, R., Pero, A., et al. (2025) · Nature · doi:10.1038/s41586-025-08864-9 · Cited by 30
Metadata
- Authors
- Traunmüller, L., Gomez, A. M., Nguyen, T.-M., & Scheiffele, P.
- Venue
- Science
- Published
- 2016-05-20
- Volume
- 352
- Issue
- 6288
- Pages
- 982-986
- ISSN
- 0036-8075
- 1095-9203
- Cited by
- 148
- References
- 6
- Language
- en
- Funders
- Boehringer Ingelheim Fonds
- European Molecular Biology Organization
- International PhD Program University of Basel
- Swiss National Science Foundation
- European Autism Interventions EU-AIMS
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.