More than 30% of the proteome in eukaryotes is comprised of intrinsically disordered proteins (IDPs) that do not fold into stable tertiary structures, even in the presence of chaperones. Given their abundance in key cellular regulators such as transcription factors (TFs) and RNA-binding proteins (RBPs), IDPs are emerging as key regulators of cell state in health and disease. This makes IDPs promising therapeutic targets in a plethora of diseases, including cancer and neurodegenerative disorders. However, the structural plasticity of IDPs and limited insights into the molecular mechanisms of IDP function are major barriers to the development of drugs targeting IDPs. In my presentation, I will talk about how we serendipitously discovered a new paradigm for drugging IDPs ‘in the pack’ of biomolecular condensates (specifically nucleoli) and contrast this with our efforts to understand ‘lone wolf’ IDPs (specifically TDP43) that seemingly do not need to phase separate in order to perform their primary functions.

Talk by:
Broder Schmidt
Stanford University School of Medicine

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