In a virtual ceremony hosted by the American Brain Foundation on April 29, Potamkin Philanthropies awarded the 2020 Potamkin Prize for Research in Pick’s, Alzheimer’s, and Related Diseases to J. Paul Taylor from St. Jude Children’s Research Hospital, Memphis, Tennessee. The $100,000 award recognizes Taylor’s contributions to the study of ALS, FTD, and other neurodegenerative disorders. Taylor is a regular contributor to Alzforum news and discussion.

J. Paul Taylor

As a neurologist, Taylor grew increasingly frustrated at the lack of effective treatments for his patients, so he began to devote more time to basic research.  His work lead to the identification of genetic variants in the gene for valosin-containing protein and in the genes for the RNA-binding proteins hnRNPA2B1 and hnRNPA1, all of which increase a person’s risk for developing neurodegenerative conditions such as Parkinsonism, amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and Paget’s disease (Mar 2013 newsMar 2013 news). 

Taylor recognized that these genetic variants accelerated a process called liquid-liquid phase separation (LLPS), whereby proteins condense into liquid droplets inside the cytoplasm, much like a yolk isolates itself inside the white of an egg. The recognition of this phenomenon spawned a new field of study. Scientists went on to find that a wide range of proteins linked to neurodegeneration can undergo LLPS, including the ALS/FTD proteins FUS and TDP-43, as well as tau, which forms the neurofibrillary tangles found in Alzheimer’s disease (May 2017 conference news). 

While LLPS is the biological process by which RNA stress granules and the nucleolus form, Taylor recognized that these droplets can also create the ideal environment for irreversible aggregation of protein (Oct 2015 news). 

Taylor’s group went on to show that ALS mutations in TDP-43 scupper the transport of essential RNA granules, and that poly-dipeptide repeats generated by a hexanucleotide expansion in the C9ORF72 ALS/FTD gene impair assembly of these membrane-less organelles (Feb 2014 newsOct 2016 news). With Rosa Rademakers at the Mayo Clinic, Jackonsville, Florida, he found that mutations in another RNA-binding protein, TIA1, increase the risk for ALD/FTD and these variants also promote liquid-liquid phase separation (Aug 2017 news). 

In a collaboration with Jim Shorter’s group at the University of Pennsylvania, Philadelphia, he reported that nuclear import proteins act as “disaggregases” to break down these liquid organelles. This is now an active area of research for therapeutic approaches (Apr 2018 news). 

In accepting his award via Zoom, Taylor announced a new translational initiative to accelerate research into neurodegenerative diseases, based on the same St. Jude model that has been successful in finding treatments for pediatric cancer.—Tom Fagan


  1. Congratulations, Paul!

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News Citations

  1. Protein Destroying Muscle, Bone, Nerves Parks on Mitochondria
  2. Disease Mutations Zip Lock Stress Granules in Proteinopathy, ALS
  3. Protein Liquid-Liquid Phase Transitions: The Science Is About to Gel
  4. Do Membraneless Organelles Host Fibril Nucleation?
  5. Escort Service: A Cytoplasmic Role for TDP-43
  6. ALS Research ‘Gels’ as Studies Tie Disparate Genetic Factors Together
  7. Newest ALS/FTD Gene Keeps Spotlight on Stress Granules
  8. Liquid Phase Transition: A Deluge of Data Points to Multiple Regulators

Further Reading

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