title: Hsp104 gives clients the individual attention they need.
abstract: Yeast heat shock protein 104 (Hsp104), the only known eukaryotic disaggregase, remodels both disordered protein aggregates and cross-β sheet amyloids. To handle this diverse clientele, DeSantis et al. report that Hsp104 hexamers use distinct mechanisms-individual subunits are able to dissolve disordered aggregates, but global subunit cooperativity is required to untangle amyloids.
authors.affiliation: Department of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: amurray@scripps.edu.
authors.forename: Amber N
authors.initials: AN
authors.lastname: Murray
authors.affiliation: Department of Chemistry, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA; Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. Electronic address: jkelly@scripps.edu.
authors.forename: Jeffery W
authors.initials: JW
authors.lastname: Kelly