2023
DOI: 10.1042/bst20221468
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The multiple ubiquitination mechanisms in CFTR peripheral quality control

Abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-regulated anion channel, which is expressed on the apical plasma membrane (PM) of epithelial cells. Mutations in the CFTR gene cause cystic fibrosis (CF), one of the most common genetic diseases among Caucasians. Most CF-associated mutations result in misfolded CFTR proteins that are degraded by the endoplasmic reticulum quality control (ERQC) mechanism. However, the mutant CFTR reaching the PM through therapeutic agents is still ubiquiti… Show more

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Cited by 4 publications
(8 citation statements)
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“…Partially unfolded CFTR at the PM (e.g., corrected ∆F508-CFTR) is subjected to ubiquitination in post-Golgi compartments and recognized by ubiquitin-dependent endosomal sorting machinery to reroute the channel from the recycling pathway toward lysosomal degradation [98,103]. While chaperone machinery (i.e., Hsc70/Hsp90) functions to maintain the properly folded CFTR conformation at the PM, structurally unstable CFTR (such as of misfolded and/or rescued mutant CFTR protein) has a reduced half-life [104,105]. This is due to modifications caused by members of the chaperone-dependent ubiquitination machinery in a process referred to as the peripheral quality control (PeriQC) system [104][105][106].…”
Section: Cftr Surfaceome and Peripheral Quality Controlmentioning
confidence: 99%
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“…Partially unfolded CFTR at the PM (e.g., corrected ∆F508-CFTR) is subjected to ubiquitination in post-Golgi compartments and recognized by ubiquitin-dependent endosomal sorting machinery to reroute the channel from the recycling pathway toward lysosomal degradation [98,103]. While chaperone machinery (i.e., Hsc70/Hsp90) functions to maintain the properly folded CFTR conformation at the PM, structurally unstable CFTR (such as of misfolded and/or rescued mutant CFTR protein) has a reduced half-life [104,105]. This is due to modifications caused by members of the chaperone-dependent ubiquitination machinery in a process referred to as the peripheral quality control (PeriQC) system [104][105][106].…”
Section: Cftr Surfaceome and Peripheral Quality Controlmentioning
confidence: 99%
“…While chaperone machinery (i.e., Hsc70/Hsp90) functions to maintain the properly folded CFTR conformation at the PM, structurally unstable CFTR (such as of misfolded and/or rescued mutant CFTR protein) has a reduced half-life [104,105]. This is due to modifications caused by members of the chaperone-dependent ubiquitination machinery in a process referred to as the peripheral quality control (PeriQC) system [104][105][106]. The PeriQC system removes non-native proteins from the PM for lysosomal degradation by ubiquitination to preserve the cell permeability barrier [106].…”
Section: Cftr Surfaceome and Peripheral Quality Controlmentioning
confidence: 99%
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