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• W2611497617 abstract "Over 170 different mutations in the gene encoding SOD1 all cause amyotrophic lateral sclerosis (ALS). Available studies have been primarily focused on the mechanisms underlying mutant SOD1 cytotoxicity. How cells defend against the cytotoxicity remains largely unknown. Here, we show that misfolding of ALS-linked SOD1 mutants and wild-type (wt) SOD1 exposes a normally buried nuclear export signal (NES)-like sequence. The nuclear export carrier protein CRM1 recognizes this NES-like sequence and exports misfolded SOD1 to the cytoplasm. Antibodies against the NES-like sequence recognize misfolded SOD1, but not native wt SOD1 both in vitro and in vivo. Disruption of the NES consensus sequence relocalizes mutant SOD1 to the nucleus, resulting in higher toxicity in cells, and severer impairments in locomotion, egg-laying, and survival in Caenorhabditis elegans. Our data suggest that SOD1 mutants are removed from the nucleus by CRM1 as a defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus." @default.
• W2611497617 created "2017-05-12" @default.
• W2611497617 creator A5011023696 @default.
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• W2611497617 date "2017-05-02" @default.
• W2611497617 modified "2023-10-02" @default.
• W2611497617 title "Nuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus" @default.
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• W2611497617 doi "https://doi.org/10.7554/elife.23759" @default.
• W2611497617 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5449186" @default.
• W2611497617 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28463106" @default.
• W2611497617 hasPublicationYear "2017" @default.
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