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Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), the dysfunctional Cl(-) channel in Cystic Fibrosis, undergoes complex biosynthesis at the endoplasmic reticulum involving several molecular chaperones including Hsp70 and many co-chaperones. Bcl-2- associated athanogenes (BAGs) constitute a protein family sharing an Hsc70-binding domain. BAG-1 possesses an ubiquitin-like domain (Ub-LD) responsible for proteasomal association and for promoting substrate release from Hsc70/Hsp70 in vitro by accelerating the chaperone ATP/ADP exchange rate.

BAG-1 Stabilizes Mutant F508del-CFTR in a Ubiquitin-Like-Domain-Dependent Manner