| First Author | Ash PE | Year | 2014 |
| Journal | Brain Res | Volume | 1584 |
| Pages | 52-8 | PubMed ID | 25108040 |
| Mgi Jnum | J:217558 | Mgi Id | MGI:5614534 |
| Doi | 10.1016/j.brainres.2014.05.052 | Citation | Ash PE, et al. (2014) Pathological stress granules in Alzheimer's disease. Brain Res 1584:52-8 |
| abstractText | 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. |
