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.
Skip Nav Destination
Article navigation
October 2012
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
- PDF Icon PDF LinkEditorial Board
Review Article|
September 26 2012
Control of amyloid assembly by autoregulation
Michael Landreh;
Michael Landreh
*Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden
Search for other works by this author on:
Jan Johansson;
Jan Johansson
†KI-Alzheimer's Disease Research Center, NVS Department, Karolinska Institutet, S-141 86 Stockholm, Sweden
‡Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, S-751 23 Uppsala, Sweden
Search for other works by this author on:
Anna Rising;
Anna Rising
†KI-Alzheimer's Disease Research Center, NVS Department, Karolinska Institutet, S-141 86 Stockholm, Sweden
‡Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, S-751 23 Uppsala, Sweden
Search for other works by this author on:
Jenny Presto;
Jenny Presto
†KI-Alzheimer's Disease Research Center, NVS Department, Karolinska Institutet, S-141 86 Stockholm, Sweden
Search for other works by this author on:
Hans Jörnvall
Hans Jörnvall
1
*Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden
1To whom correspondence should be addressed (email Hans.Jornvall@ki.se).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
June 06 2012
Revision Received:
July 09 2012
Accepted:
July 23 2012
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2012 Biochemical Society
2012
Biochem J (2012) 447 (2): 185–192.
Article history
Received:
June 06 2012
Revision Received:
July 09 2012
Accepted:
July 23 2012
Citation
Michael Landreh, Jan Johansson, Anna Rising, Jenny Presto, Hans Jörnvall; Control of amyloid assembly by autoregulation. Biochem J 15 October 2012; 447 (2): 185–192. doi: https://doi.org/10.1042/BJ20120919
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.