ArticleNature communications2018
Structural basis of trans-synaptic interactions between PTPδ and SALMs for inducing synapse formation.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Alternative microexon splicing code for a four-amino acid peptide of PTPRD governs behavioral development.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-wide association study of social isolation in 63,497 Japanese individuals from the general population.Translational psychiatry · 2026Article
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Synaptic and Non-Synaptic Functions of PTPRD: A Receptor Tyrosine Phosphatase at the Crossroads of Neural Circuitry and Metabolism.Journal of neurochemistry · 2025Review
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.Research square · 2025Article
- Alternatively spliced mini-exon B in PTPδ regulates excitatory synapses through cell-type-specific trans-synaptic PTPδ-IL1RAP interaction.Nature communications · 2025Article
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.bioRxiv : the preprint server for biology · 2025Article
- Transcriptomic Changes and Pathological Mechanisms in Familial and Sporadic Idiopathic Restless Legs Syndrome: Implications for Inflammation and Cell Adhesion Molecules.Nature and science of sleep · 2025Article
- Disrupted hypothalamic transcriptomics and proteomics in a mouse model of type 2 diabetes exposed to recurrent hypoglycaemia.Diabetologia · 2024Article
- Comparative Genomic Analysis Identifies Great-Ape-Specific Structural Variants and Their Evolutionary Relevance.Molecular biology and evolution · 2023Article
- LRFN5 and OLFM4 as novel potential biomarkers for major depressive disorder: a pilot study.Translational psychiatry · 2023Article
- Mice lacking Ptprd exhibit deficits in goal-directed behavior and female-specific impairments in sensorimotor gating.PloS one · 2023Article
- Developmental synapse pathology triggered by maternal exposure to the herbicide glufosinate ammonium.Frontiers in molecular neuroscience · 2023Article
- 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
- SALM4 negatively regulates NMDA receptor function and fear memory consolidation.Communications biology · 2021Article
- Canonical versus non-canonical transsynaptic signaling of neuroligin 3 tunes development of sociality in mice.Nature communications · 2021Article
- LAR Receptor Tyrosine Phosphatase Family in Healthy and Diseased Brain.Frontiers in cell and developmental biology · 2021Review
- A Human IgSF Cell-Surface Interactome Reveals a Complex Network of Protein-Protein Interactions.Cell · 2020Article
- Splice-dependent trans-synaptic PTPδ-IL1RAPL1 interaction regulates synapse formation and non-REM sleep.The EMBO journal · 2020Article
- Further confirmation of netrin 1 receptor (DCC) as a depression risk gene via integrations of multi-omics data.Translational psychiatry · 2020Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPδ-SALM2 and PTPδ-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPδ, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPδ. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPδ-SALM5 requires the dimeric property of SALM5.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.