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Splicing is the process by which eukaryotic RNA is edited before its translation into protein. The RNA strand transcribed from eukaryotic DNA is called the primary transcript. The primary transcripts that become mRNAs are called precursor messenger RNAs (pre-mRNAs). Eukaryotic pre-mRNA contains alternating sequences of exons and introns. Exons are nucleotide sequences that code for proteins, whereas introns are the non-coding regions. In RNA splicing, introns are removed and exons are bonded...
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Mutation of the ALS-/FTD-Associated RNA-Binding Protein FUS Affects Axonal Development.

Francesca W van Tartwijk1, Lucia C S Wunderlich1, Ioanna Mela1

  • 1Department of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge CB3 0AS, United Kingdom.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|May 1, 2024
PubMed
Summary
This summary is machine-generated.

Mutant fused in sarcoma (FUS) protein causes axonal branching defects in a frog model, impacting neurodevelopment in diseases like ALS and FTD. This study reveals FUS

Keywords:
ALS/FTDFUSaxonal branchingcytoskeletongrowth coneneurodevelopment

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • Aberrant RNA-binding protein (RBP) fused in sarcoma (FUS) condensation and localization are implicated in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD).
  • Altered RBP function is linked to axonal cytoskeletal organization and branching changes in neurodevelopmental disorders.

Purpose of the Study:

  • To investigate whether branching defects occur in vivo in a model of FUS-associated neurodegenerative disease.
  • To determine the impact of specific FUS mutations on axonal development and cytoskeletal integrity.

Main Methods:

  • Utilized two Xenopus models expressing ALS/FTD-associated FUS mutants: FUS(P525L) and FUS(16R).
  • Assessed axonal complexity and branching in vivo.
  • Examined axonal cytoskeletal integrity in vitro using fluorescence and atomic force microscopy.

Main Results:

  • Both FUS mutants significantly reduced axonal complexity in vivo.
  • FUS(P525L) exhibited an axon looping defect, suggesting errors in stop cue signaling.
  • Mutant FUS decreased actin density in the growth cone, altering its mechanical properties in vitro.

Conclusions:

  • FUS mutations impair axonal development by affecting cytoskeletal integrity and potentially disrupting axonal guidance cues.
  • These findings provide in vivo evidence for FUS-associated axonal defects, contributing to the understanding of ALS and FTD pathogenesis.