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- W2415662204 abstract "Abstract The neuromuscular junction (NMJ) allows the transformation of a neuronal message into a mechanical force by muscle contraction and is the target of several neuromuscular disorders. While the neuronal side is under extensive research, the muscle appeared recently to have a growing role in the formation and integrity of the neuromuscular junction. We used an in vitro model of mature myofibers to study the role of dynein on major postsynaptic proteins. We found that dynein affects the expression and the clustering of acetylcholine receptors (AChRs), muscle specific tyrosine kinase (MuSK) and Rapsyn. We also show that myofibers with dynein impairment or from an amyotrophic lateral sclerosis (ALS) model (SOD1 G93A ) show similar defects in myofiber formation and agrin-induced AChR clustering suggesting a role for dynein impairment in ALS progression. Finally, we found that dynein can affect MuSK traffic through the endosomal pathway. Collectively, our studies show that defects in dynein can lead to impairment of muscle NMJ components’ expression and clustering. We propose that NMJ defects could happen via defective MuSK traffic and that this could be one of the pathological features involved in neurodegeneration such as ALS." @default.
- W2415662204 created "2016-06-24" @default.
- W2415662204 creator A5017237197 @default.
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- W2415662204 creator A5025688861 @default.
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- W2415662204 creator A5038365822 @default.
- W2415662204 date "2016-06-10" @default.
- W2415662204 modified "2023-10-16" @default.
- W2415662204 title "Dynein disruption perturbs post-synaptic components and contributes to impaired MuSK clustering at the NMJ: implication in ALS" @default.
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- W2415662204 doi "https://doi.org/10.1038/srep27804" @default.
- W2415662204 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4901269" @default.
- W2415662204 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27283349" @default.
- W2415662204 hasPublicationYear "2016" @default.
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