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• W2131370644 startingPage "942" @default.
• W2131370644 abstract "Mutations in the superoxide dismutase 1 (sod1) gene cause familial amyotrophic lateral sclerosis (FALS), likely due to the toxic properties of misfolded mutant SOD1 protein. Here we demonstrated that, starting from the pre-onset stage of FALS, misfolded SOD1 species associates specifically with kinesin-associated protein 3 (KAP3) in the ventral white matter of SOD1G93A-transgenic mouse spinal cord. KAP3 is a kinesin-2 subunit responsible for binding to cargos including choline acetyltransferase (ChAT). Motor axons in SOD1G93A-Tg mice also showed a reduction in ChAT transport from the pre-onset stage. By employing a novel FALS modeling system using NG108-15 cells, we showed that microtubule-dependent release of acetylcholine was significantly impaired by misfolded SOD1 species. Furthermore, such impairment was able to be normalized by KAP3 overexpression. KAP3 was incorporated into SOD1 aggregates in human FALS cases as well. These results suggest that KAP3 sequestration by misfolded SOD1 species and the resultant inhibition of ChAT transport play a role in the dysfunction of ALS." @default.
• W2131370644 created "2016-06-24" @default.
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• W2131370644 date "2008-12-16" @default.
• W2131370644 modified "2023-09-28" @default.
• W2131370644 title "Mutant SOD1 impairs axonal transport of choline acetyltransferase and acetylcholine release by sequestering KAP3" @default.
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• W2131370644 doi "https://doi.org/10.1093/hmg/ddn422" @default.
• W2131370644 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2640210" @default.
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