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English
Cooperative assembly and misfolding of CFTR domains in vivo.
scientific article published on 28 January 2009
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2663924
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20 January 2020
title
Cooperative assembly and misfolding of CFTR domains in vivo
(English)
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20 January 2020
author
Gergely L Lukacs
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2
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20 January 2020
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Kai Du
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20 January 2020
publication date
28 January 2009
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20 January 2020
published in
Molecular Biology of the Cell
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20 January 2020
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20
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20 January 2020
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7
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20 January 2020
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1903-1915
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20 January 2020
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Assembly and misassembly of cystic fibrosis transmembrane conductance regulator: folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of membrane spanning domain (MSD) 1 and MSD2
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Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding
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Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
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CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices
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Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
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Revertant mutants G550E and 4RK rescue cystic fibrosis mutants in the first nucleotide-binding domain of CFTR by different mechanisms
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Phosphorylation of CFTR by PKA promotes binding of the regulatory domain
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Assembly of functional CFTR chloride channels
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Side chain and backbone contributions of Phe508 to CFTR folding
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COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
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Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
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Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes
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Severed molecules functionally define the boundaries of the cystic fibrosis transmembrane conductance regulator's NH(2)-terminal nucleotide binding domain
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Multiple membrane-cytoplasmic domain contacts in the cystic fibrosis transmembrane conductance regulator (CFTR) mediate regulation of channel gating
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The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR.
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Limited proteolysis as a probe for arrested conformational maturation of delta F508 CFTR
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Kinetic stabilisation of a modular protein by domain interactions
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based on heuristic
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Removal of multiple arginine-framed trafficking signals overcomes misprocessing of delta F508 CFTR present in most patients with cystic fibrosis
1 reference
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1091/MBC.E08-09-0950
1 reference
stated in
Europe PubMed Central
PMCID
2663924
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19176754%20AND%20SRC:MED&resulttype=core&format=json
retrieved
20 January 2020
PMCID
2663924
1 reference
stated in
Europe PubMed Central
PMCID
2663924
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19176754%20AND%20SRC:MED&resulttype=core&format=json
retrieved
20 January 2020
PubMed ID
19176754
1 reference
stated in
Europe PubMed Central
PMCID
2663924
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19176754%20AND%20SRC:MED&resulttype=core&format=json
retrieved
20 January 2020
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