Co-translational folding of the first transmembrane domain of ABC-transporter CFTR is supported by assembly with the first cytosolic domain
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Summary
The first stages of co-translational domain folding and assembly of CFTR, the ABC-transporter defective in the most abundant rare inherited disease cystic fibrosis, are revealed, involving structures conserved in type-I ABC exporters.
- Type
- preprint
- Published
- 2020-12-20
- Cited by
- 45
- References
- 86
- Access
- Open access
- OpenAlex
- https://openalex.org/W3117584059
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:232376611
Keywords
Transmembrane domain, Transmembrane protein, Cyclic nucleotide-binding domain, Cytosol, Folding (DSP implementation)
References
- Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator.
- CFTR Folding Consortium: Methods Available for Studies of CFTR Folding and Correction
- The cystic fibrosis transmembrane regulator is present and functional in endosomes. Role as a determinant of endosomal pH.
- Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
- Alteration of the Cystic Fibrosis Transmembrane Conductance Regulator Folding Pathway
- Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins.
- The delta F508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane. Determination of functional half-lives on transfected cells.
- The translocation, folding, assembly and redox-dependent degradation of secretory and membrane proteins in semi-permeabilized mammalian cells.
- Molecular models of the open and closed states of the whole human CFTR protein
- An Electrostatic Interaction at the Tetrahelix Bundle Promotes Phosphorylation-dependent Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Channel Opening*
- A microtiter plate assay for the characterization of serine proteases by their esterase activity.
- Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis.
- Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening.
- Function, pharmacological correction and maturation of new Indian CFTR gene mutations.
- Defining the disease liability of variants in the cystic fibrosis transmembrane conductance regulator gene
- Correctors of F508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein
- Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Potentiator VX-770 (Ivacaftor) Opens the Defective Channel Gate of Mutant CFTR in a Phosphorylation-dependent but ATP-independent Manner* ♦
- Identification of the cystic fibrosis gene: Cloning and characterization of complementary DNA
- Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function
- The ΔF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
Cited by
- CFTR corrector efficacy is associated with occupancy of distinct binding sites
- Mechanism of CFTR correction by type I folding correctors
- A Precision Medicine Approach to Optimize Modulator Therapy for Rare CFTR Folding Mutants
- Pharmacological chaperones improve intra-domain stability and inter-domain assembly via distinct binding sites to rescue misfolded CFTR
- Cystic Fibrosis Transmembrane Conductance Regulator Folding Mutations Reveal Differences in Corrector Efficacy Linked to Increases in Immature Cystic Fibrosis Transmembrane Conductance Regulator Expression
- In silico and functional characterisation of an ultra-rare CFTR mutation identifies novel lasso motif interactions regulating channel gating
- Revisiting CFTR Interactions: Old Partners and New Players
- Molecular dynamics and functional characterization of I37R-CFTR lasso mutation provide insights into channel gating activity
- One Size Does Not Fit All: The Past, Present and Future of Cystic Fibrosis Causal Therapies
- Molecular mechanisms of cystic fibrosis – how mutations lead to misfunction and guide therapy
- CFTR Rescue by Lumacaftor (VX-809) Induces an Extensive Reorganization of Mitochondria in the Cystic Fibrosis Bronchial Epithelium
- Structure basis of CFTR folding, function and pharmacology.
- Mechanism of dual pharmacological correction and potentiation of human CFTR
- Molecular Structures Reveal Synergistic Rescue of Δ508 CFTR by Trikafta Modulators
- Redefining Hypo- and Hyper-Responding Phenotypes of CFTR Mutants for Understanding and Therapy
- Acting on the CFTR Membrane-Spanning Domains Interface Rescues Some Misfolded Mutants
- ABC-transporter CFTR folds with high fidelity through a modular, stepwise pathway
- Changes in cystic fibrosis transmembrane conductance regulator protein expression prior to and during elexacaftor-tezacaftor-ivacaftor therapy
- Post-approval studies with the CFTR modulators Elexacaftor-Tezacaftor—Ivacaftor
- A Novel, Uniquely Efficacious Type of CFTR Corrector with Complementary Mode of Action
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