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Brain Res. 2014 Oct 10;1584:52-8. doi: 10.1016/j.brainres.2014.05.052. Epub 2014 Aug 7.

Pathological stress granules in Alzheimer's disease.

Author information

1
Depts. of Pharmacology and Neurology, Boston University School of Medicine, Boston, MA 02118, United States.
2
Depts. of Pharmacology and Neurology, Boston University School of Medicine, Boston, MA 02118, United States. Electronic address: bwolozin@bu.edu.

Abstract

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.

KEYWORDS:

Alzheimer’s disease; G3BP1; Pathological stress granules; TIA-1; Tau

PMID:
25108040
PMCID:
PMC4256948
DOI:
10.1016/j.brainres.2014.05.052
[Indexed for MEDLINE]
Free PMC Article

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