期刊
ACS CHEMICAL NEUROSCIENCE
卷 13, 期 17, 页码 2544-2546出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschemneuro.2c00480
关键词
Nucleocytoplasmic transport; amyotrophic lateral sclerosis; ALS/FTLD; Nup62; proteinopathy; TDP-43; FG-Nups; TDP-43 condensates
资金
- Indian Council of Medical Research (ICMR) , Government of India, India [52/06/2020/BIO/BMS]
- DST-INSPIRE
Nucleocytoplasmic transport is impaired in C9-ALS/FTLD, and a protein called FG-Nup62 is found to be mislocalized and colocalized with TDP-43, promoting its transition from liquid to solid state. This study highlights the involvement of Nup62 in the pathogenesis of ALS/FTLD and its interaction with TDP-43.
The nucleocytoplasmic transport (NCT) is impaired in C9-ALS/FTLD, a common genetically caused form of ALS and FTLD. The NCT is regulated by proteins called FG-nucleoporins (FG-Nups), with domains enriched in phenylalanine-glycine repeats. However, the relationship between FG-Nups and TDP-43, an RBP found to be mislocalized in ALS/FTLD patients, has not been defined. A recent study found that a critical protein, FG-Nup62, is mislocalized both in vivo and in vitro in diseased states. The mislocalized Nup62 was colocalized with TDP-43 in cytoplasmic inclusions and promoted its liquid-to-solid transition. The work highlights the involvement of Nup62 in the pathogenesis of ALS/FTLD and the interaction between Nup62 and TDP-43.
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