Control of amyloid assembly by autoregulation.
Biochem J
; 447(2): 185-92, 2012 Oct 15.
Article
en En
| MEDLINE
| ID: mdl-23013511
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Homeostasis
/
Amiloide
Tipo de estudio:
Etiology_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Biochem J
Año:
2012
Tipo del documento:
Article
País de afiliación:
Suecia