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    Pathogenic tau in Alzheimer's disease disrupts memory by blocking protein synthesis in neurons. Targeting the tau-eIF4B interaction restores synaptic plasticity and memory formation.

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    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Cell Biology

    Background:

    • Synaptic plasticity is crucial for memory formation but is impaired in tauopathies like Alzheimer's disease (AD).
    • Pathogenic tau accumulation in neurons obstructs synaptic plasticity, leading to memory loss, but the precise mechanism remains unclear.

    Purpose of the Study:

    • To elucidate how pathogenic tau inhibits synaptic plasticity and causes memory deficits.
    • To identify the molecular targets and pathways involved in tau-mediated synaptic dysfunction.

    Main Methods:

    • Analysis of the plasticity-associated translatome in Frontotemporal lobar degeneration with tau inclusions (FTLD-tau) neurons.
    • Investigating the interaction between pathogenic tau and the translation initiation factor eIF4B.
    • Assessing the impact of modulating tau-eIF4B interaction on dendritic protein synthesis and synaptic plasticity.

    Main Results:

    • FTLD-tau inhibits synaptic plasticity by blocking activity-dependent protein synthesis in neuronal dendrites.
    • Pathogenic tau binds to eIF4B, causing its dissociation from the translation initiation complex and reducing its levels in dendrites.
    • Restoring eIF4B levels or inhibiting the tau-eIF4B interaction rescued local protein synthesis and synaptic plasticity in FTLD-tau neurons.

    Conclusions:

    • Pathogenic tau binding to eIF4B disrupts the local synthesis of essential plasticity-related proteins.
    • This disruption in protein synthesis impairs synapse strengthening and memory formation in tauopathies.
    • Targeting the tau-eIF4B interaction presents a potential therapeutic strategy for memory loss in AD and related disorders.