bioRxivNeurosciencePreprint
Title: Cell-autonomous and non-cell-autonomous effects of TRIM72 on ALS disease progression
Xue ZhangiD, Ji HeiD, Ning SongiD, Xipeng LiiD, Weizhe WangiD, Yueting Hu, Qing Li, Yiqing HuiD, Chunmu Yin, Peng ZhaoiD, Xinyi JiangiD, Xuejiao PiaoiD, Dawei Meng, Hongmei Cheng, Zhaohui CheniD, Xusheng HuangiD, Yu PaniD, Xinming QiiD, Jin ReniD, Li LuoiD, Lin Peng, Wei Peng GuoiD, Tong WangiD, Haipeng GongiD, Dongsheng FaniD, Yichang JiaiD
Abstract
Dysfunction of RNA-binding proteins, including TDP-43 and FUS, has been associated with amyotrophic lateral sclerosis (ALS); however, the underlying mechanisms are largely unknown. Here, we reported that a neuronal upregulation of TRIM72 (Tripartite Motif Containing 72) in FUS mutation knockin ALS models slows disease progression. TRIM72 interacts with Commander, a protein complex for recycling of membrane proteins, facilitating membrane repair and antioxidation. Exosomal TRIM72 is detected in ALS patient cerebrospinal fluid (CSF) and extracellular application of exosomal TRIM72 protects cell from membrane damage. In a sporadic ALS cohort, CSF TRIM72 level associates ALS disease progression. AAV-mediated neuronal expression of TRIM72 slows down the disease progressions in ALS models and in an ALS patient without adverse effects over a year treatment course. Taken together, our results suggest a universal neuronal protection of a TRIM family protein in cell-autonomous and non-cell-autonomous manners in ALS.
- organism: human
- assay: proteomics
- research focus: drug response / drug discovery
- approach: experimental assay
- Citations
- 3
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- ALS mice carrying pathological mutant TDP-43, but not mutant FUS, display axonal transport defects in vivo
James N. Sleigh, Andrew Paul Tosolini, … Giampietro Schiavo·Cell ReportsPeer-reviewed·Mar 1, 2020
- Cdc48/VCP and endocytosis regulate TDP-43 and FUS toxicity and turnover
Guangbo Liu, Aaron T. Byrd, … J. Ross Buchan·Molecular and Cellular BiologyPeer-reviewed·Nov 22, 2019
- Wild-type FUS corrects ALS-like disease induced by cytoplasmic mutant FUS through autoregulation.
Inmaculada Sanjuan-Ruiz, Noé Govea-Perez, … Luc Dupuis·Molecular NeurodegenerationPeer-reviewed·Sep 6, 2021
- Two neuronal models of TDP-43 proteinopathy display reduced axonal translation, increased oxidative stress, and defective exocytosis.
Alessandra Pisciottani, Laura Croci, … G. Giacomo Consalez·Frontiers in Cellular NeurosciencePeer-reviewed·Nov 13, 2023
- Single-cell RNA sequencing across isogenic FUS and TARDBP ALS lines reveals a shared early mitochondrial dysfunction unique to motor neurons.
Christoph Schweingruber, Jik Nijssen, … Eva Hedlund·Nature CommunicationsPeer-reviewed·May 19, 2025
- An ALS-associated mutation in human FUS reduces neurotransmission from C. elegans motor neurons to muscles
Sebastian M. Markert, Michael Skoruppa, … Christian Stigloher·Biology OpenPeer-reviewed·Jan 1, 2020