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TDP-43/FUS in motor neuron disease: Complexity and challenges
Erika N Guerrero1,2,3, Haibo Wang1, Joy Mitra1
1Department of Radiation Oncology, Houston Methodist Research Institute, Houston, Texas 77030, USA.
Progress in Neurobiology
|October 4, 2016
Summary
Amyotrophic lateral sclerosis (ALS) involves motor neuron death. This review explores how TAR DNA-binding protein-43 (TDP-43) and fused in sarcoma (FUS) DNA binding may contribute to ALS pathogenesis.
Area of Science:
- Neuroscience
- Molecular Biology
- Genetics
Background:
- Amyotrophic lateral sclerosis (ALS) is a motor neuron disease with diverse subtypes.
- TDP-43 and FUS protein dysfunction are implicated in ALS pathogenesis.
- While RNA binding is studied, their DNA binding roles in ALS are less understood.
Purpose of the Study:
- To review ALS subtypes and etiopathologies.
- To discuss the role of TDP-43 and FUS in motor neuron disease.
- To highlight the potential significance of their DNA binding function in ALS.
Main Methods:
- Literature review of ALS pathogenesis.
- Analysis of studies on TDP-43 and FUS protein functions.
- Discussion of genomic damage and DNA repair in ALS.
Main Results:
- TDP-43 and FUS proteins exhibit nuclear clearance and cytoplasmic aggregation in ALS.
- Genomic damage is observed in TDP-43 and FUS-linked ALS.
- FUS is associated with neuronal DNA damage repair pathways.
Conclusions:
- Deregulated DNA binding of TDP-43 and FUS may play a critical role in ALS.
- Further research into their DNA binding functions is crucial for understanding ALS.
- Understanding these mechanisms could lead to new therapeutic strategies for ALS.
