ReviewFrontiers in cellular neuroscience2020
Synaptic Organizers in Alzheimer's Disease: A Classification Based on Amyloid-β Sensitivity.
Review in Frontiers in cellular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 14 citations in OpenAlex.
- PLCG2 downregulation impairs synaptic function and increases Alzheimer's disease hallmarks in neuronal cultures.Nature genetics · 2026Article
- Canonical Pathways Rewiring in Alzheimer's Disease.International journal of molecular sciences · 2026Article
- Non-microglial downregulation ofbioRxiv : the preprint server for biology · 2026Article
- Differences in blood levels of neuroligin-derived peptides in a cohort for early detection of Alzheimer's disease.The journals of gerontology. Series A, Biological sciences and medical sciences · 2026Article
- Molecular and neuropathological determinants of neuronal dysfunction in Alzheimer's disease.bioRxiv : the preprint server for biology · 2025Article
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.Research square · 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
- Dystroglycan-HSPG interactions provide synaptic plasticity and specificity.Glycobiology · 2024Review
- Genome-wide epistasis analysis reveals gene-gene interaction network on an intermediate endophenotype P-tau/AβScientific reports · 2024Article
- Ferroptosis: underlying mechanisms and involvement in neurodegenerative diseases.Apoptosis : an international journal on programmed cell death · 2024Review
- Role of Neurexins in Alzheimer's Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- α-Synuclein Preformed Fibrils Bind to β-Neurexins and Impair β-Neurexin-Mediated Presynaptic Organization.Cells · 2023Article
- SorCS1 inhibits amyloid-β binding to neurexin and rescues amyloid-β-induced synaptic pathology.Life science alliance · 2023Article
- Correlation of Ferroptosis and Other Types of Cell Death in Neurodegenerative Diseases.Neuroscience bulletin · 2022Review
- Key Disease Mechanisms Linked to Alzheimer's Disease in the Entorhinal Cortex.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synaptic pathology is one of the major hallmarks observed from the early stage of Alzheimer's disease (AD), leading to cognitive and memory impairment characteristic of AD patients. Synaptic connectivity and specificity are regulated by multiple trans-bindings between pre- and post-synaptic organizers, the complex of which exerts synaptogenic activity. Neurexins (NRXs) and Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are the major presynaptic organizers promoting synaptogenesis through their distinct binding to a wide array of postsynaptic organizers. Recent studies have shown that amyloid-β oligomers (AβOs), a major detrimental molecule in AD, interact with NRXs and neuroligin-1, an NRX-binding postsynaptic organizer, to cause synaptic impairment. On the other hand, LAR-RPTPs and their postsynaptic binding partners have no interaction with AβOs, and their synaptogenic activity is maintained even in the presence of AβOs. Here, we review the current evidence regarding the involvement of synaptic organizers in AD, with a focus on Aβ synaptic pathology, to propose a new classification where NRX-based and LAR-RPTP-based synaptic organizing complexes are classified into Aβ-sensitive and Aβ-insensitive synaptic organizers, respectively. We further discuss how their different Aβ sensitivity is involved in Aβ vulnerability and tolerance of synapses for exploring potential therapeutic approaches for AD.
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