Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
Volume 1832, Issue 8, Pages 1271-1278Publisher
ELSEVIER
DOI: 10.1016/j.bbadis.2013.04.011
Keywords
Amyloid; Functional amyloid; Protein aggregate; Neurodegenerative disease; RNA granule
Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan [24111542, 22110004, 24657093, 22240037]
- CREST from Japan Science and Technology Agency
- Research Committee for Ataxic Diseases from MHLW
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [22240037, 24111542, 25253066, 24657093, 24659436, 22110004] Funding Source: KAKEN
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Many proteins exhibit propensities to form fibrillar aggregates called amyloids that are rich in beta-sheet structures. Abnormal accumulation of amyloids in the brain and spinal cords is well known as a major pathological change in neurodegenerative diseases; therefore, amyloids have long been considered as disease culprits formed via protein misfolding and should be avoided in healthy cells. Recently, however, increasing numbers of proteins have been identified that require formation of fibrillar states for exertion of their physiological functions, and the critical roles of such functional amyloids include a molecular switch for environmental adaptation, a structural template for catalysis, and a regulator of intracellular signaling. Protein amyloids will, therefore, he more prevailed in our physiologies than we have expected so far. Here, we have reviewed recent studies on such regulatory roles of protein fibrillar aggregates in various physiologies and further discussed possible relations of functional to pathological amyloids. (C) 2013 Elsevier B.V. All rights reserved.
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