title: Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases.
abstract: Many proteins exhibit propensities to form fibrillar aggregates called amyloids that are rich in β-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, be 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.
authors.affiliation: Department of Chemistry, Keio University,Yokohama, Kanagawa 223-8522, Japan. furukawa@chem.keio.ac.jp
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Furukawa
authors.forename: Nobuyuki
authors.initials: N
authors.lastname: Nukina
mesh_terms: D000682:Amyloid / Q000235:genetics / Q000378:metabolism*; D000686:Amyloidosis / Q000235:genetics* / Q000378:metabolism*; D000818:Animals; D006801:Humans; D019636:Neurodegenerative Diseases / Q000235:genetics* / Q000378:metabolism*; D017510:Protein Folding; D012313:RNA / Q000235:genetics* / Q000378:metabolism
chemical_list: D000682:Amyloid; D012313:RNA