Emerging role of Alzheimer's disease-associated ubiquilin-1 in protein aggregation.

Abstract:

:Abnormal protein aggregation and intracellular or extracellular accumulation of misfolded and aggregated proteins are key events in the pathogenesis of different neurodegenerative diseases. Furthermore, endoplasmic reticulum stress and impairment of the ubiquitin-proteasome system probably contribute to neurodegeneration in these diseases. A characteristic feature of AD (Alzheimer's disease) is the abnormal accumulation of Abeta (amyloid beta-peptide) in the brain. Evidence shows that the AD-associated PS (presenilin) also forms aggregates under certain conditions and that another AD-associated protein, ubiquilin-1, controls protein aggregation and deposition of aggregated proteins. Here, we review the current knowledge of ubiquilin-1 and PS in protein aggregation and related events that potentially influence neurodegeneration.

journal_name

Biochem Soc Trans

authors

Haapasalo A,Viswanathan J,Bertram L,Soininen H,Tanzi RE,Hiltunen M

doi

10.1042/BST0380150

subject

Has Abstract

pub_date

2010-02-01 00:00:00

pages

150-5

issue

Pt 1

eissn

0300-5127

issn

1470-8752

pii

BST0380150

journal_volume

38

pub_type

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