Johansson, Jan
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
Abstract
The assembly of proteins into amyloid fibrils can be an element of both protein aggregation diseases and a functional unit in healthy biological pathways. In both cases, it must be kept under tight control to prevent undesired aggregation. In normophysiology, proteins can self-chaperone amyloidogenic segments by restricting their conformational flexibility in an overall stabilizing protein fold. However, some aggregation-prone segments cannot be controlled in this manner and require additional regulatory elements to limit fibrillation. The present review summarizes different molecular mechanisms that proteins use to control their own assembly into fibrils, such as the inclusion of a chaperoning domain or a blocking segment in the proform, the controlled release of an amyloidogenic region from the folded protein, or the adjustment of fibrillation propensity according to pH. Autoregulatory elements can control disease-related as well as functional fibrillar protein assemblies and distinguish a group of self-regulating amyloids across a wide range of biological functions and organisms.
Keywords
BRICHOS domain; HET-S prion; hydrophobin; melanin synthesis; proinsulin C-peptide; protein misfolding; self-chaperoning; spider silk
Published in
Biochemical Journal
2012, volume: 447, pages: 185-192
Publisher: PORTLAND PRESS LTD
SLU Authors
Rising, Anna
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
Presto, Jenny
- Karolinska Institute
UKÄ Subject classification
Cell and Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1042/BJ20120919
Permanent link to this page (URI)
https://res.slu.se/id/publ/42659