ArticleIn vitro cellular & developmental biology. Animal2015
Autophagy-linked FYVE protein (Alfy) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS).
Article in In vitro cellular & developmental biology. Animal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Fisetin Attenuates Mutant SOD1 Aggregation in Amyotrophic Lateral Sclerosis via Nrf2-Mediated Autophagy Activation.Journal of molecular neuroscience : MN · 2025Article
- ALFY localizes to early endosomes and cellular protrusions to facilitate directional cell migration.Journal of cell science · 2022Article
- Cromolyn sodium delays disease onset and is neuroprotective in the SOD1Scientific reports · 2019Article
- Lysosomal dysfunction in proteinopathic neurodegenerative disorders: possible therapeutic roles of cAMP and zinc.Molecular brain · 2019Review
- Review
- The Neuroprotection of Low-Dose Morphine in Cellular and Animal Models of Parkinson's Disease Through Ameliorating Endoplasmic Reticulum (ER) Stress and Activating Autophagy.Frontiers in molecular neuroscience · 2018Article
- Wheat germ agglutinin-induced paraptosis-like cell death and protective autophagy is mediated by autophagy-linked FYVE inhibition.Oncotarget · 2017Article
- The autophagy scaffold protein ALFY is critical for the granulocytic differentiation of AML cells.Scientific reports · 2017Article
- Autophagy in neurodegenerative diseases: from mechanism to therapeutic approach.Molecules and cells · 2015Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Autophagy-linked FYVE (Alfy) is a protein implicated in the selective degradation of aggregated proteins. In our present study, we found that Alfy was recruited into the aggregated G93A-SOD1 in transgenic mice with amyotrophic lateral sclerosis (ALS). We demonstrated that Alfy overexpression could decrease the expression of mutant proteins via the autophagosome-lysosome pathway, and thereby, the toxicity of mutant proteins was reduced. The clearance of the mutant proteins in NSC34 cells was significantly inhibited in an Alfy knockdown cellular model. We therefore deduced that Alfy translocalization likely is involved in the pathogenesis of ALS. Alfy may be developed into a useful target for ALS therapy.
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