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α-Synuclein emulsifies TDP-43 prion-like domain-RNA liquid droplets to promote heterotypic amyloid fibrils

Commun Biol. 2023-12; 
Shailendra Dhakal, Malay Mondal, Azin Mirzazadeh, Siddhartha Banerjee, Ayanjeet Ghosh, Vijayaraghavan Rangachari
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Proteins, Expression, Isolation and Analysis … Wild-type plasmids were synthesized from Genscript ? and the rest of the constructs were cloned at Florida State University. All proteins were expresed in E. coli BL21 (DE3) star cells (… Get A Quote

摘要

Many neurodegenerative diseases including frontotemporal lobar degeneration (FTLD), Lewy body disease (LBD), multiple system atrophy (MSA), etc., show colocalized deposits of TDP-43 and α-synuclein (αS) aggregates. To understand whether these colocalizations are driven by specific molecular interactions between the two proteins, we previously showed that the prion-like C-terminal domain of TDP-43 (TDP-43PrLD) and αS synergistically interact to form neurotoxic heterotypic amyloids in homogeneous buffer conditions. However, it remains unclear if αS can modulate TDP-43 present within liquid droplets and biomolecular condensates called stress granules (SGs). Here, using cell culture and in vitro TDP-43PrLD - RN... More

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