Amyloids are insoluble fibrillar protein deposits with an underlying cross-β structure initially discovered in the context of human diseases. However, it is now clear that the same fibrillar structure is used by many organisms, from bacteria to humans, in order to achieve a diverse range of biological functions. These functions include structure and protection (e.g. curli and chorion proteins, and insect and spider silk proteins), aiding interface transitions and cell–cell recognition (e.g. chaplins, rodlins and hydrophobins), protein control and storage (e.g. Microcin E492, modulins and PMEL), and epigenetic inheritance and memory [e.g. Sup35, Ure2p, HET-s and CPEB (cytoplasmic polyadenylation element-binding protein)]. As more examples of functional amyloid come to light, the list of roles associated with functional amyloids has continued to expand. More recently, amyloids have also been implicated in signal transduction [e.g. RIP1/RIP3 (receptor-interacting protein)] and perhaps in host defence [e.g. aDrs (anionic dermaseptin) peptide]. The present chapter discusses in detail functional amyloids that are used in Nature by micro-organisms, non-mammalian animals and mammals, including the biological roles that they play, their molecular composition and how they assemble, as well as the coping strategies that organisms have evolved to avoid the potential toxicity of functional amyloid.
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Review Article| August 18 2014
Functional amyloid: widespread in Nature, diverse in purpose
Chi L.L. Pham ;
Ann H. Kwan ;
Margaret Sunde 1
*Discipline of Pharmacology, School of Medical Sciences, University of Sydney, NSW 2006, Australia
†School of Molecular Bioscience, University of Sydney, NSW 2006, Australia
1To whom correspondence should be addressed (email firstname.lastname@example.org).
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Essays Biochem (2014) 56: 207–219.
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Sarah Perrett, Chi L.L. Pham, Ann H. Kwan, Margaret Sunde; Functional amyloid: widespread in Nature, diverse in purpose. Essays Biochem 18 August 2014; 56 207–219. doi: https://doi.org/10.1042/bse0560207
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