Journal
JOURNAL OF CELL BIOLOGY
Volume 201, Issue 3, Pages 361-372Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201302044
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Funding
- Ellison Medical Foundation New Scholar in Aging Award
- National Institutes of Health (NIH) Director's New Innovator Award [DP2OD002177, DP2OD004417]
- NIH [R01GM099836, R21NS067354, R21HD074510, R01NS065317, R01NS073660]
- NIH Medical Scientist Training Program
- Paul and Daisy Soros Fellowship for New Americans
- Packard Center for ALS Research at Johns Hopkins University
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Amyotrophic 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.
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