Journal
BRAIN RESEARCH
Volume 1584, Issue -, Pages 52-58Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.brainres.2014.05.052
Keywords
Pathological stress granules; Tau; TIA-1; G3BP1; Alzheimer's disease
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Funding
- NIA NIH HHS [R01 AG050471] Funding Source: Medline
- NIEHS NIH HHS [R01 ES020395] Funding Source: Medline
- NIGMS NIH HHS [T32 GM008541] Funding Source: Medline
- NINDS NIH HHS [R01 NS089544, R21 NS073679, R21 NS066108] Funding Source: Medline
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A feature of neurodegenerative disease is the accumulation of insoluble protein aggregates in the brain. In some conditions, including Amyotrophic Lateral Sclerosis and Frontotemporal lobar degeneration, the primary aggregating entities are RNA binding proteins. Through regulated prion-like assembly, RNA binding proteins serve many functions in RNA metabolism that are essential for the healthy maintenance of cells of the central nervous system. Those RNA binding proteins that are the core nucleating factors of stress granules (SGs), including TIA-1, TIAR, TTP and G3BP1, are also found in the pathological lesions of other neurological conditions, such as Alzheimer's disease, where the hallmark aggregating protein is not an RNA binding protein. This discovery suggests that the regulated cellular pathway, which utilizes assembly of RNA binding proteins to package and silence mRNAs during stress, may be integral in the aberrant pathological protein aggregation that occurs in numerous neurodegenerative conditions. This article is part of a Special Issue entitled RNA Metabolism 2013. (C) 2014 Elsevier B.V. All rights reserved.
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