[HTML][HTML] A chaperone pathway in protein disaggregation: Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
AG Cashikar, M Duennwald, SL Lindquist - Journal of Biological Chemistry, 2005 - ASBMB
Cellular protein folding is challenged by environmental stress and aging, which lead to
aberrant protein conformations and aggregation. One way to antagonize the detrimental
consequences of protein misfolding is to reactivate vital proteins from aggregates. In the
yeast Saccharomyces cerevisiae, Hsp104 facilitates disaggregation and reactivates
aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40 (Ydj1). The small heat
shock proteins, Hsp26 and Hsp42, also function in the recovery of misfolded proteins and …
aberrant protein conformations and aggregation. One way to antagonize the detrimental
consequences of protein misfolding is to reactivate vital proteins from aggregates. In the
yeast Saccharomyces cerevisiae, Hsp104 facilitates disaggregation and reactivates
aggregated proteins with assistance from Hsp70 (Ssa1) and Hsp40 (Ydj1). The small heat
shock proteins, Hsp26 and Hsp42, also function in the recovery of misfolded proteins and …
