Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP.

@article{Kundrat2010IdentificationOR,
  title={Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP.},
  author={Lenka Kundrat and Lynne Regan},
  journal={Journal of molecular biology},
  year={2010},
  volume={395 3},
  pages={587-94}
}
Molecular chaperones Hsp70 and Hsp90 are in part responsible for maintaining the viability of cells by facilitating the folding and maturation process of many essential client proteins. The ubiquitin ligase C-terminus of Hsc70 interacting protein (CHIP) has been shown in vitro and in vivo to associate with Hsp70 and Hsp90 and ubiquitinate them, thus targeting them to the proteasome for degradation. Here, we study one facet of this CHIP-mediated turnover by determining the lysine residues on… CONTINUE READING
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