NTD – RRM Stacking

We are pleased to announce that our latest TDP-43 study has been published: Identifying interactions between TDP-43’s N-terminal and RNA-binding domains. In this Protein Science publication, we present 2D NMR experiments showing allosteric shifts in the RNA‑binding surfaces of the RRMs in the presence of NTD. Carr-Purcell-Meiboom-Gill (CPMG)-NMR results also support NTD interaction with the RRMs and protein‑protein docking presents several possible sites of interaction. Further, we show that NTD modulates affinity for RNA, supporting regulatory role for NTD in TDP‑43 – RNA interactions.

Congrats to all!

Au revoir NY, bonjour Gainesville Florida!

After two fruitful years at NYU, it's time for a change to the sunnier and greener Gainesville! Alongside my dedicated research team, I'm thrilled to embrace the role of Assistant Dean in Innovation and Entrepreneurship. Excited to launch innovative initiatives!

New Pub: HspA5 and TDP43

Congrats to Liberty and co-authors on their publication Heat shock protein Grp78/BiP/HspA5 binds directly to TDP-43 and mitigates toxicity associated with disease pathology in Scientific Reports!

Using proximity-dependent biotin identification (BioID), the authors discovered several Hsp70 isoforms that associated with TPD-43. They then showed that HspA5 bound specifically with the RNA-binding domain of TDP-43. They also found that HspA5 was upregulated in a Drosophila model of ALS and in human prefrontal cortex neurons from ALS patient donors. Excitingly, they show that overexpression of HspA5 in the Drosophila ALS model rescued TDP-43-induced toxicity, suggesting that upregulation of HspA5 may have a compensatory role in ALS pathobiology.