Document TypeJournal Article
KeywordsAmyotrophic Lateral Sclerosis
Nerve Tissue Proteins
Protein Structure, Tertiary
RNA-Binding Protein FUS
Nervous System Diseases
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AbstractAmyotrophic lateral sclerosis (ALS) is a fatal human neurodegenerative disease affecting primarily motor neurons. Two RNA-binding proteins, TDP-43 and FUS, aggregate in the degenerating motor neurons of ALS patients, and mutations in the genes encoding these proteins cause some forms of ALS. TDP-43 and FUS and several related RNA-binding proteins harbor aggregation-promoting prion-like domains that allow them to rapidly self-associate. This property is critical for the formation and dynamics of cellular ribonucleoprotein granules, the crucibles of RNA metabolism and homeostasis. Recent work connecting TDP-43 and FUS to stress granules has suggested how this cellular pathway, which involves protein aggregation as part of its normal function, might be coopted during disease pathogenesis.
SourceLi YR, King OD, Shorter J, Gitler AD. Stress granules as crucibles of ALS pathogenesis. J Cell Biol. 2013 Apr 29;201(3):361-72. doi: 10.1083/jcb.201302044. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/50576
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