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Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA.
Phenylalanine-508 mediates a cytoplasmic–membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
- Adrian W. R. Serohijos, T. Hegedűs, J. Riordan
- BiologyProceedings of the National Academy of Sciences
- 4 March 2008
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).
Erratum: Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNA
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.
Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
CFTR function and prospects for therapy.
- J. Riordan
- BiologyAnnual review of biochemistry
- 2 June 2008
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.
Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis
Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
- M. Loo, T. Jensen, Liying Cui, Yue‐xian Hou, X. Chang, J. Riordan
- BiologyThe EMBO journal
- 1 December 1998
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.
Permeability of Wild-Type and Mutant Cystic Fibrosis Transmembrane Conductance Regulator Chloride Channels to Polyatomic Anions
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.
Domain interdependence in the biosynthetic assembly of CFTR.
COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
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.