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• W2000291566 abstract "Mutations in the Cu,Zn-superoxide dismutase (SOD1) gene cause 20–25% of familial amyotrophic lateral sclerosis (ALS). Mutant SOD1 causes motor neuron degeneration through toxic gain-of-function(s). However, the direct molecular targets of mutant SOD1, underlying its toxicity, are not fully understood. In this study, we found that α/β-tubulin is one of the major mutant SOD1-interacting proteins, but that wild-type SOD1 does not interact with it. The interaction between tubulin and mutant SOD1 was detected in the spinal cords of mutant G93A SOD1 transgenic mice before the onset of symptoms. Tubulin interacted with amino acid residues 1–23 and 116–153 of SOD1. Overexpression of mutant SOD1 resulted in the accumulation of tubulin in detergent-insoluble fractions. In a cell-free system, mutant SOD1 modulated tubulin polymerization, while wild-type SOD1 did not. Since tightly regulated microtubule dynamics is essential for neurons to remain viable, α/β-tubulin could be an important direct target of mutant SOD1." @default.
• W2000291566 created "2016-06-24" @default.
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• W2000291566 date "2009-09-01" @default.
• W2000291566 modified "2023-09-26" @default.
• W2000291566 title "Familial amyotrophic lateral sclerosis-linked mutant SOD1 aberrantly interacts with tubulin" @default.
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• W2000291566 doi "https://doi.org/10.1016/j.bbrc.2009.06.138" @default.
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