Encyclopedia of Biophysics

Living Edition
| Editors: Gordon Roberts, Anthony Watts, European Biophysical Societies

Functional Amyloid

  • Margaret Sunde
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-35943-9_181-1

Introduction

Functional amyloid is a fibrillar protein assembly with the same structural, morphological, and dye-binding properties that characterize disease-causing or disease-associated amyloid fibrils but whose production or application is beneficial to the organism and not associated with protein misfolding or pathology (Pham et al. 2014). Proteins that form functional amyloid contain amyloidogenic motifs that provide self-assembly capability and the biologically active form of the protein is retained or generated in the fibrillar form (Fig. 1). The amyloid, multimeric version of the protein has properties beyond that of the monomeric component protein. In functional amyloid structures, the self-assembly properties of amyloid fibrils, and the stability and resistance to proteolysis of the amyloid structure, are applied for a wide range of biological functions including production of protective coatings, development of mechanical strength, control of cytotoxic intermediates,...
This is a preview of subscription content, log in to check access.

References

  1. Hennig S et al (2015) Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles. J Cell Biol 210:529–539.  https://doi.org/10.1083/jcb.201504117CrossRefPubMedPubMedCentralGoogle Scholar
  2. Lindquist S (1997) Mad cows meet psi-chotic yeast: the expansion of the prion hypothesis. Cell 89:495–498CrossRefPubMedGoogle Scholar
  3. Loquet A, Saupe SJ (2017) Diversity of amyloid motifs in NLR signaling in Fungi. Biomol Ther 7.  https://doi.org/10.3390/biom7020038
  4. Pham CL, Kwan AH, Sunde M (2014) Functional amyloid: widespread in Nature, diverse in purpose. Essays Biochem 56:207–219.  https://doi.org/10.1042/bse0560207. 2014/08/19 ednCrossRefPubMedGoogle Scholar
  5. Wu H, Fuxreiter M (2016) The structure and dynamics of higher-order assemblies: amyloids signalosomes, and granules. Cell 165:1055–1066.  https://doi.org/10.1016/j.cell.2016.05.004CrossRefPubMedPubMedCentralGoogle Scholar

Copyright information

© European Biophysical Societies' Association (EBSA) 2018

Authors and Affiliations

  1. 1.Pharmacology, School of Medical Sciences, Faculty of Medicine and Health and Sydney NanoUniversity of SydneySydneyAustralia