. A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation. Cell. 2015 Aug 27;162(5):1066-77. PubMed.


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  1. Increasing attention has focused on the liquid droplet nature of RNA-binding proteins. This physico-chemical characteristic has been well-known by RNA biologists for decades. However, the role of liquid gel transitions has come to the fore in neurodegeneration research because it could well play an important role in the pathophysiology of motor neuron diseases, and possibly other neurodegenerative diseases.

    In this elegant paper, a team led by Hyman and Alberti takes this liquid gel transition model and shows that disease-linked mutations in FUS accelerate the transition to an aggregated solid state, which can then become persistent and pathological.  

    The team also highlights the role of PARPs in the phase transition. This adds an important new dimension to the approaches we need to use when evaluating these systems. This work provides a nice mixture of physical/chemical as well as cell biology to the field of neurodegenerative diseases, and is well done.

    View all comments by Benjamin Wolozin

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