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Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA.
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Phenylalanine-508 mediates a cytoplasmic–membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
TLDR
A 3D structure of CFTR is presented, constructed by molecular modeling and supported biochemically, in which Phe-508 mediates a tertiary interaction between the surface of NBD1 and a cytoplasmic loop (CL4) in the C-terminal membrane-spanning domain (MSD2).
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Erratum: Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNA
TLDR
A deletion of three base pairs that results in the omission of a phenylalanine residue at the center of the first predicted nucleotide-binding domain was detected in CF patients.
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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
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CFTR function and prospects for therapy.
  • J. Riordan
  • Biology
    Annual review of biochemistry
  • 2 June 2008
TLDR
This review considers different therapeutic strategies that have arisen from knowledge of CFTR structure and function as well as its biosynthetic processing, intracellular trafficking, and turnover.
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Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
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Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
TLDR
This work shows the first direct evidence of a role for Hsp90 in the maturation of a newly synthesized integral membrane protein by interaction with its cytoplasmic domains on the ER surface.
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Permeability of Wild-Type and Mutant Cystic Fibrosis Transmembrane Conductance Regulator Chloride Channels to Polyatomic Anions
TLDR
Permeability ratios followed a lyotropic sequence, suggesting that permeability is dependent on ionic hydration energies, and site-directed mutagenesis of two adjacent threonines in TM6 to smaller, less polar alanines led to a significant increase in single channel conductance and elevated permeability to several large anions.
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Domain interdependence in the biosynthetic assembly of CFTR.
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COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
TLDR
It is proposed that the di-acidic exit code plays a key role in linking CFTR to the COPII coat machinery and is the primary defect responsible for CF in ΔF508-expressing patients.
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