The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

By G. C. Meacham, C. Patterson, Wenyue Zhang, J. M. Younger, D. Cyr. Nature Cell Biology, 2000

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Ubiquitin: structures, functions, mechanisms. (2004, background): “CHIP substrates that conform to this paradigm include the cystic fibrosis transmembrane receptor [112], the glucocorticoid receptor [113], and tau [114,115].”
Handbook of ion channels (2015, background): “The quality control of CFTR is performed in the ER membrane and the cytoplasmic compartment (Meacham et al., 2001; Younger et al., 2004, 2006).”
The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. (2002, background): “An important ERAD component is the yeast chaperone Kar2 (352) and its mammalian homolog BiP (205), and also the Hsc70 cochaperone CHIP (303) that appears to be an E3 that acts along with chaperones to ubiquitinate misfolded proteins (see above).”
Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. (2006, background): “…recruitment of components such as CHIP and the regulatory factors HspBP1 and Bag that bind the Hsc-Hsp70/40 complex and target CFTR to 812 Cell 127, 803–815, November 17, 2006 ª2006 Elsevier Inc. ERAD (Alberti et al., 2004; Dai et al., 2005; Meacham et al., 2001; Younger et al., 2006) (Figure 7A).”