@article{THESIS,
      recid = {3576},
      author = {Yoo, Haneul},
      title = {Chaperones Remodel Stress-Induced Biomolecular  Condensates},
      publisher = {University of Chicago},
      school = {Ph.D.},
      address = {2021-12},
      number = {THESIS},
      pages = {115},
      abstract = {Stresses such as heat shock trigger formation of protein  aggregates and induction of a disaggregation system  composed of molecular chaperones. Recent work reveals that  several cases of apparent heat-induced aggregation, long  thought to be the result of toxic misfolding, instead  reflect evolved, adaptive biomolecular condensation, with  chaperone activity contributing to condensate regulation.  Here I show that the yeast disaggregation system directly  disperses heat-induced biomolecular condensates of  endogenous poly(A)-binding protein (Pab1) orders of  magnitude more rapidly than aggregates of the most commonly  used misfolded model substrate, firefly luciferase. Beyond  its efficiency, heat-induced condensate dispersal differs  from heat-induced aggregate dispersal in its molecular  requirements and mechanistic behavior. This work  establishes a bona fide endogenous heat-induced substrate  for long-studied heat shock proteins, rigorously isolates a  specific example of chaperone regulation of condensates,  and underscores needed expansion of the proteotoxic  interpretation of the heat shock response to encompass  adaptive, chaperone-mediated regulation.},
      url = {http://knowledge.uchicago.edu/record/3576},
      doi = {https://doi.org/10.6082/uchicago.3576},
}