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SUMMARY:Predicting protein condensation from sequence: new and widespread 
 roles for condensates in physiology and disease - Steven Boeynams (Baylor 
 College of Medicine)
DTSTART:20231012T133000Z
DTEND:20231012T141000Z
UID:TALK204913@talks.cam.ac.uk
DESCRIPTION:In the last decade it has become increasingly clear that biomo
 lecular condensates are widespread within cells. Besides membranebound com
 partments\, these assemblies constitute a powerful and versatile way for t
 he cell to compartmentalize and orchestrate its internal biochemistry. Whi
 le the number of validated scaffold and client proteins has steadily grown
 \, how this behavior is actually encoded in sequence remains understudied.
  Since transmembrane domains can be pretty accurately predicted from seque
 nce\, similar efforts have been explored for condensate proteins. Most of 
 the current prediction tools unfortunately rely on the available in vitro 
 data for condensation. As the field initially focused on prion-like domain
 s\, the resulting predictions are often biased towards such sequences. Man
 y condensates do not rely on such prion-like domains though\, but typicall
 y come in different flavors of their chemical space. Here we leveraged a s
 imple paradigm of complex coacervation to probe such additional chemistrie
 s. Using ex vivo enrichment strategies coupled to mass spectrometry-based 
 proteomics\, we unbiasedly uncover a whole new set of candidate condensate
  proteins. Training a machine learning algorithm on this dataset allows us
  to predict such behavior with surprising accuracy from sequence. This app
 roach allowed us to uncover a whole new set of uncharacterized condensate 
 proteins with essential functions to human cells. Additionally\, our algor
 ithm predicts that condensation behavior is pervasive&mdash\;not only with
 in&mdash\;but also outside of cells. We unexpectedly uncover novel and evo
 lutionary conserved roles for condensation in animal physiology\, ranging 
 from innate immune and venom systems to biomaterials and biofluids. Severa
 l of these protein classes and their condensation-driving features are rap
 idly evolving\, arguing that phase separation is not merely an epiphenomen
 on but a core functional mechanism under direct selective pressure.&nbsp\;
LOCATION:Seminar Room 1\, Newton Institute
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