ArticleThe Journal of biological chemistry2008
The SALM family of adhesion-like molecules forms heteromeric and homomeric complexes.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 58 citations in OpenAlex.
- LRFN5 locus structure is associated with autism and influenced by the sex of the individual and locus conversions.Autism research : official journal of the International Society for Autism Research · 2022Article
- Article
- SALM4 negatively regulates NMDA receptor function and fear memory consolidation.Communications biology · 2021Article
- Dynamic bi-directional phosphorylation events associated with the reciprocal regulation of synapses during homeostatic up- and down-scaling.Cell reports · 2021Article
- Sorting nexin-27 regulates AMPA receptor trafficking through the synaptic adhesion protein LRFN2.eLife · 2021Article
- Of Molecules and Mechanisms.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020Review
- SALM1 controls synapse development by promoting F-actin/PIP2-dependent Neurexin clustering.The EMBO journal · 2019Article
- Molecular dissection of cone photoreceptor-enriched genes encoding transmembrane and secretory proteins.Journal of neuroscience research · 2019Article
- Lrfn2-Mutant Mice Display Suppressed Synaptic Plasticity and Inhibitory Synapse Development and Abnormal Social Communication and Startle Response.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Leucine-rich repeat-containing synaptic adhesion molecules as organizers of synaptic specificity and diversity.Experimental & molecular medicine · 2018Review
- Structural basis of SALM5-induced PTPδ dimerization for synaptic differentiation.Nature communications · 2018Article
- Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation.Nature communications · 2018Article
- Pathophysiology of Trans-Synaptic Adhesion Molecules: Implications for Epilepsy.Frontiers in cell and developmental biology · 2018Review
- SALM/Lrfn Family Synaptic Adhesion Molecules.Frontiers in molecular neuroscience · 2018Review
- Autism-like behaviours and enhanced memory formation and synaptic plasticity in Lrfn2/SALM1-deficient mice.Nature communications · 2017Article
- A novel synaptic junction preparation for the identification and characterization of cleft proteins.PloS one · 2017Article
- SALM4 suppresses excitatory synapse development by cis-inhibiting trans-synaptic SALM3-LAR adhesion.Nature communications · 2016Article
- SALM5 trans-synaptically interacts with LAR-RPTPs in a splicing-dependent manner to regulate synapse development.Scientific reports · 2016Article
- Splicing-Dependent Trans-synaptic SALM3-LAR-RPTP Interactions Regulate Excitatory Synapse Development and Locomotion.Cell reports · 2015Article
- Electron microscopic tomography reveals discrete transcleft elements at excitatory and inhibitory synapses.Frontiers in synaptic neuroscience · 2015Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Synaptic adhesion-like molecules (SALMs) are a newly discovered family of adhesion molecules that play roles in synapse formation and neurite outgrowth. The SALM family is comprised of five homologous molecules that are expressed largely in the central nervous system. SALMs 1-3 contain PDZ-binding domains, whereas SALMs 4 and 5 do not. We are interested in characterizing the interactions of the SALMs both among the individual members and with other binding partners. In the present study, we focused on the interactions formed by the five SALM members in rat brain and heterologous cells. In brain, we found that SALMs 1-3 strongly co-immunoprecipitated with each other, whereas SALMs 4 and 5 did not, suggesting that SALMs 4 and 5 mainly form homomeric complexes. In heterologous cells transfected with SALMs, co-immunoprecipitation studies showed that all five SALMs form heteromeric and homomeric complexes. We also determined if SALMs could form trans-cellular associations between transfected heterologous cells. Both SALMs 4 and 5 formed homophilic, but not heterophilic associations, whereas no trans associations were formed by the other SALMs. The ability of SALM4 to form trans interactions is due to its extracellular N terminus because chimeras of SALM4 N terminus and SALM2 C terminus can form trans interactions, whereas chimeras of SALM2 N terminus and SALM4 C terminus cannot. Co-culture experiments using HeLa cells and rat hippocampal neurons expressing the SALMs showed that SALM4 is recruited to points of contact between the cells. In neurons, these points of contact were seen in both axons and dendrites.
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