TDP-43 Mutations in Familial and Sporadic Amyotrophic Lateral Sclerosis

Jemeen Sreedharan, Ian P. Blair, Vineeta B. Tripathi, Xun Hu, Caroline Vance, Boris Rogelj, Steven Ackerley, Jennifer C. Durnall, Kelly L. Williams, Emanuele Buratti,

Science · 2008 · 2.6K citations · 24 references

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TL;DR

Amyotrophic lateral sclerosis is a fatal motor neuron disorder marked by ubiquitinated TDP‑43 inclusions, yet the protein’s function and its mechanistic role in neurodegeneration remain unclear. The study uncovered pathogenic TARDBP mutations in a conserved region that segregate with ALS, fragment more readily than wild type, induce neural apoptosis and developmental delay, and provide evidence for a pathophysiological link between TDP‑43 and ALS.

Abstract

Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disorder characterized pathologically by ubiquitinated TAR DNA binding protein (TDP-43) inclusions. The function of TDP-43 in the nervous system is uncertain, and a mechanistic role in neurodegeneration remains speculative. We identified neighboring mutations in a highly conserved region of TARDBP in sporadic and familial ALS cases. TARDBPM337V segregated with disease within one kindred and a genome-wide scan confirmed that linkage was restricted to chromosome 1p36, which contains the TARDBP locus. Mutant forms of TDP-43 fragmented in vitro more readily than wild type and, in vivo, caused neural apoptosis and developmental delay in the chick embryo. Our evidence suggests a pathophysiological link between TDP-43 and ALS.

References

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