Nuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus
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Summary
It is suggested that S OD1 mutants are removed from the nucleus by CRM1 as a defense mechanism against proteotoxicity of misfolded SOD1 in the nucleus.
- Type
- article
- Published
- 2017-05-02
- Cited by
- 37
- References
- 68
- Access
- Open access
- OpenAlex
- https://openalex.org/W2611497617
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4668867
Keywords
SOD1, Cell biology, Proteotoxicity, Mutant, Nuclear export signal
References
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- The role of heat shock proteins in Amyotrophic Lateral Sclerosis: The therapeutic potential of Arimoclomol.
- CRM1-mediated Recycling of Snurportin 1 to the Cytoplasm
- Toxicity of ALS-linked SOD1 mutants.
- Nuclear bodies in neurodegenerative disease.
- Molecular chaperones in cellular protein folding: the birth of a field.
- RNA interference-mediated silencing of mutant superoxide dismutase rescues cyclosporin A-induced death in cultured neuroblastoma cells.
- Degradation of Amyotrophic Lateral Sclerosis-linked Mutant Cu,Zn-Superoxide Dismutase Proteins by Macroautophagy and the Proteasome*
- Design of peptide inhibitors for the importin alpha/beta nuclear import pathway by activity-based profiling.
- An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis
- Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1.
- SOD1 Mutations Targeting Surface Hydrogen Bonds Promote Amyotrophic Lateral Sclerosis without Reducing Apo-state Stability*
- Dorfin Ubiquitylates Mutant SOD1 and Prevents Mutant SOD1-mediated Neurotoxicity*
- Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form
- SOD1 as a molecular switch for initiating the homeostatic ER stress response under zinc deficiency.
Cited by
- MIF inhibits the formation and toxicity of misfolded SOD1 amyloid aggregates: implications for familial ALS
- Modulation of Fluorescent Protein Chromophores To Detect Protein Aggregation with Turn-On Fluorescence
- Distinct proteostasis circuits cooperate in nuclear and cytoplasmic protein quality control
- Thrombin and the Coag-Inflammatory Nexus in Neurotrauma, ALS, and Other Neurodegenerative Disorders
- The coming-of-age of nucleocytoplasmic transport in motor neuron disease and neurodegeneration
- Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants
- Nucleocytoplasmic transport defects in neurodegeneration - Cause or consequence?
- Nicotinamide Riboside Enhances Mitochondrial Proteostasis and Adult Neurogenesis through Activation of Mitochondrial Unfolded Protein Response Signaling in the Brain of ALS SOD1G93A Mice
- Superoxide Dismutase 1 in Health and Disease: How a Frontline Antioxidant Becomes Neurotoxic
- Nuclear Transport Deficits in Tau-Related Neurodegenerative Diseases
- The role of DNA damage response in amyotrophic lateral sclerosis
- USP7 regulates ALS-associated proteotoxicity and quality control through the NEDD4L–SMAD pathway
- Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises
- Directly converted astrocytes retain the ageing features of the donor fibroblasts and elucidate the astrocytic contribution to human CNS health and disease
- MARK2 phosphorylates eIF2α in response to proteotoxic stress
- An update to the CRM1 cargo/NES database NESdb
- Mitophagy Regulates Neurodegenerative Diseases
- RNA Molecular Signature Profiling in PBMCs of Sporadic ALS Patients: HSP70 Overexpression Is Associated with Nuclear SOD1
- Karyopherin-mediated nucleocytoplasmic transport
- Nuclear SOD1 in Growth Control, Oxidative Stress Response, Amyotrophic Lateral Sclerosis, and Cancer
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