alexa TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia.
Neurology

Neurology

Journal of Alzheimers Disease & Parkinsonism

Author(s): Mackenzie IR, Rademakers R, Neumann M

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Abstract Abnormal intracellular protein aggregates comprise a key characteristic in most neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). The seminal discoveries of accumulation of TDP-43 in most cases of ALS and the most frequent form of FTD, frontotemporal lobar degeneration with ubiquitinated inclusions, followed by identification of FUS as the novel pathological protein in a small subset of patients with ALS and various FTD subtypes provide clear evidence that these disorders are related. The creation of a novel molecular classification of ALS and FTD based on the identity of the predominant protein abnormality has, therefore, been possible. The striking functional and structural similarities of TDP-43 and FUS, which are both DNA/RNA binding proteins, imply that abnormal RNA metabolism is a pivotal event, but the mechanisms leading to TDP-43 and FUS accumulation and the resulting neurodegeneration are currently unknown. Nonetheless, TDP-43 and FUS are promising candidates for the development of novel biomarker assays and targeted therapies. Copyright © 2010 Elsevier Ltd. All rights reserved. This article was published in Lancet Neurol and referenced in Journal of Alzheimers Disease & Parkinsonism

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