Reference - Detail
| RRC ID | 85697 |
|---|---|
| Author | Bilican S, Nabawi Y, Zhang WH, Petrovic D, Wehrmann M, Muñoz-García S, Koyuncu S, Vilchez D. |
| Title | C9orf72 ALS-causing mutations lead to mislocalization and aggregation of nucleoporin Nup107 into stress granules. |
| Journal | FEBS Lett |
| Abstract |
Amyotrophic lateral sclerosis (ALS) is a fatal disorder caused by motor neuron degeneration. Hexanucleotide repeat expansions in the C9orf72 gene, the most common genetic cause of ALS (C9-ALS), drive toxicity through different mechanisms. These pathological changes include alterations in stress granules (SGs), ribonucleoprotein complexes formed under stress conditions. Here, we show that G3BP1, a core component of SGs, exhibits enhanced interaction with the nucleoporin Nup107 in motor neurons derived from patient iPSCs carrying C9orf72 mutations. Moreover, Nup107 colocalizes with SGs and aggregates in C9-ALS motor neurons. Notably, knockdown of npp-5, the Caenorhabditis elegans ortholog of Nup107, alleviates ALS-associated phenotypes in worm models, including reduced lifespan and impaired motility. Together, our findings provide insights into disease-related changes in C9-ALS pathogenesis. |
| Published | 2025-9-1 |
| DOI | 10.1002/1873-3468.70156 |
| PMID | 40891053 |
| IF | 3.057 |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | Bluesky |
| Total number of mentions | 36 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| Human and Animal Cells | CiRA00024(HPS0292) |