Stress granules as crucibles of ALS pathogenesis.

TitleStress granules as crucibles of ALS pathogenesis.
Publication TypeJournal Article
Year of Publication2013
AuthorsLi YR, King OD, Shorter J, Gitler AD
JournalThe Journal of cell biology
Volume201
Issue3
Pagination361-72
Date Published2013 Apr 29
Abstract

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.

DOI10.1002/stem.1408
Alternate JournalJ. Cell Biol.