Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases

Yoshiaki Furukawa, Nobuyuki Nukina

Research output: Contribution to journalReview article

15 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1271-1278
Number of pages8
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Volume1832
Issue number8
DOIs
Publication statusPublished - 2013 Aug 1

Keywords

  • Amyloid
  • Functional amyloid
  • Neurodegenerative disease
  • Protein aggregate
  • RNA granule

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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