. Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity. Cell Rep. 2016 May 17;15(7):1455-1466. Epub 2016 May 6 PubMed.


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  1. This paper by Vanderweyde and colleagues elegantly demonstrates a role for tau in regulating the interactions of the RNA-binding protein TIA1. In cell culture, they demonstrate that interactions between TIA1 and tau influence stress granule formation and tau-associated toxicity. A very well-controlled analysis of the TIA1 interacting proteome in brain tissue from wild-type mice and tau knockout mice indicate that tau is important for the protein interactome network of TIA1. These data are interesting because they implicate RNA-binding proteins in the pathophysiology of tauopathy.

    RNA-binding proteins contribute to the pathophysiology of ALS, and these data add to the growing body of evidence that ALS and frontotemporal dementias lie on a disease spectrum. Although tau pathology is observed in some ALS patients, genetically, tau is one of the molecules that has been thought of as “purely” on the FTD side of this spectrum. These data indicate that similar RNA-mediated mechanisms may be at play in degeneration mediated by tau and more classically ALS proteins such as TDP43 and FUS. It will be interesting to see future studies in human tissue and perhaps knock-in or regulatable models to extend and confirm these results. 

    View all comments by Tara Spires-Jones

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  1. Stress Granule Protein Entwines and Misfolds Tau