Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum–associated degradation

@inproceedings{Matsumura2011RoleOH,
  title={Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum–associated degradation},
  author={Yoshihiro Matsumura and Larry L. David and William R. Skach},
  booktitle={Molecular biology of the cell},
  year={2011}
}
The Hsp/c70 cytosolic chaperone system facilitates competing pathways of protein folding and degradation. Here we use a reconstituted cell-free system to investigate the mechanism and extent to which Hsc70 contributes to these co- and posttranslational decisions for the membrane protein cystic fibrosis transmembrane conductance regulator (CFTR). Hsc70 binding to CFTR was destabilized by the C-terminal domain of Bag-1 (CBag), which stimulates client release by accelerating ADP-ATP exchange… CONTINUE READING

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