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Updated: May 20, 2025

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C9ORF72 poly-PR disrupts expression of ALS/FTD-implicated STMN2 through SRSF7.

Karen S Wang^1,2, Julie Smeyers^1,2, Kevin Eggan^3,4

¹Institute for Neurodegenerative Diseases, University of California, San Francisco, CA, USA.

Acta Neuropathologica Communications

|March 27, 2025

Summary

This summary is machine-generated.

The C9ORF72 repeat expansion causes neurodegenerative diseases like ALS and FTD. Antisense poly-PR disrupts RNA binding proteins, reducing STMN2 and impairing axonal repair.

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Area of Science:

Neuroscience
Genetics
Molecular Biology

Background:

C9ORF72 hexanucleotide repeat expansion is a leading genetic cause of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD).
Dipeptide repeat proteins (DPRs) produced from this expansion have toxic gain-of-function effects, but their precise mechanisms of neurotoxicity are unclear.

Purpose of the Study:

To investigate the molecular mechanisms by which DPRs, specifically poly-proline-arginine (poly-PR), contribute to neurodegeneration.
To identify the cellular targets of poly-PR and their role in neuronal dysfunction, particularly axonal regeneration.

Main Methods:

Utilized human induced pluripotent stem cell (iPSC)-derived neurons.
Employed global phospho-proteomics to identify poly-PR interacting proteins.
Investigated the role of specific RNA binding proteins (RBPs) and STMN2 in axonal regeneration defects.

Main Results:

Poly-PR was found to inhibit axonal regeneration in iPSC-derived neurons.
Poly-PR selectively perturbs nuclear RNA binding proteins (RBPs).
Depletion of SRSF7, an RBP, reduced STMN2 levels and impaired axonal regeneration, which was rescued by exogenous STMN2.

Conclusions:

Antisense repeat-encoded poly-PR disrupts RBPs, notably SRSF7, leading to decreased STMN2.
This mechanism links DPR gain-of-function to STMN2 loss-of-function phenotypes, explaining axonal repair defects in C9ORF72-associated neurodegeneration.