<i>C9orf72</i> arginine‐rich dipeptide repeat proteins promote assembly and impair dynamics of processing body
Our results provide both in vitro and in vivo evidence that arginine-rich DPRs induce the spontaneous formation of PBs via LLPS. Our results also indicate that poly(GR)-induced PBs are more stable than the transient and dynamic conventional PBs. Given that PBs uniquely enriched with mRNA degradation and decay factors, the consequences of impairing these processes are expected to contribute to abnormal RNA metabolism in c9FTD/ALS.
Authors
- Monica Castanedes‐Casey (ORCID: https://orcid.org/0000-0002-8441-7801)
- Dennis W. Dickson (ORCID: https://orcid.org/0000-0001-7189-7917)
- Wei Shao (ORCID: https://orcid.org/0000-0002-8782-4904)
- Karen Jansen‐West (ORCID: https://orcid.org/0000-0002-1234-7103)
- Lillian M. Daughrity (ORCID: https://orcid.org/0000-0003-4644-7265)
- Björn Oskarsson (ORCID: https://orcid.org/0000-0002-1725-9866)
- Jorge Alaiz Noya
- Yongjie Zhang
- Yanwei Wu
- Leonard Petrucelli
- Tania F Gendron
- Caroline J. Jones
Institutions
- WinnMed (US)
- Mayo Clinic in Florida (US)
Publication Details
- Journal
- Alzheimer s & Dementia
- Published
- 2025-12-01
- DOI
- https://doi.org/10.1002/alz70861_108268
- Primary Topic
- Amyotrophic Lateral Sclerosis Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00