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Title
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Non-muscle myosin II regulates presynaptic actin assemblies and neuronal mechanobiology
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Author
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Abstract
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| Neuromuscular junctions (NMJs) are evolutionarily ancient, specialized contacts between neurons and muscles. Axons and NMJs must endure mechanical strain through a lifetime of muscle contraction, making them vulnerable to aging and neurodegenerative conditions. However, cellular strategies for mitigating this mechanical stress remain unknown. In this study, we used Drosophila larval NMJs to investigate the role of actin and myosin (actomyosin)-mediated contractility in generating and responding to cellular forces at the neuron-muscle interface. We identified a new long-lived, low-turnover presynaptic actin core traversing the NMJ, which partly co-localizes with non-muscle myosin II (NMII). Neuronal RNAi of NMII induced disorganization of this core, suggesting that this structure might have contractile properties. Interestingly, neuronal RNAi of NMII also decreased NMII levels in the postsynaptic muscle proximal to neurons, suggesting that neuronal actomyosin rearrangements propagate their effects trans-synaptically. We also observed reduced Integrin levels upon NMII knockdown, indicating that neuronal actomyosin disruption triggers rearrangements of Integrin-mediated connections between neurons and surrounding muscle tissue. In summary, our study identifies a previously uncharacterized presynaptic actomyosin subpopulation that upholds the neuronal mechanical continuum, transmits signals to adjacent muscle tissue, and collaborates with Integrin receptors to govern the mechanobiology of the neuromuscular junction. |
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Language
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English
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Publication
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BioRxiv
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2023
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DOI
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10.1101/2023.11.10.566609
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Volume/pages
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(2023)
, p. 1-34
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Pubmed ID
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38014140
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Full text (Publisher's DOI)
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Full text (open access)
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