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Article

Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.

Nature communications - 30 Aug 2017

Bagdany Miklos, Veit Guido, Fukuda Ryosuke, Avramescu Radu G, Okiyoneda Tsukasa, Baaklini Imad, Singh Jay, Sovak Guy, Xu Haijin, Apaja Pirjo M, Sattin Sara, Beitel Lenore K, Roldan Ariel, Colombo Giorgio, Balch William, Young Jason C, Lukacs Gergely L

Abstract excerpt

Molecular chaperones are pivotal in folding and degradation of the cellular proteome but their impact on the conformational dynamics of near-native membrane proteins with disease relevance remains unknown. Here we report the effect of chaperone activity on the functional conformation of the temperature-sensitive mutant cystic fibrosis channel (∆F508-CFTR) at the plasma membrane and after reconstitution into...

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Share to Cell Membrane
Share to Cystic Fibrosis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to HSC70 Heat-Shock Proteins

Share to HSP90 Heat-Shock Proteins

Share to Molecular Chaperones

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Source

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Identifiers

PMID: 28855508
DOI: 10.1038/s41467-017-00444-4
PMCID: PMC5577305

Genes

CFTR

Provenance

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Related research

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Research trail→

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Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.PMID 28855508Read ↗

ATP-dependent thermoring basis for the heat unfolding of the first nucleotide-binding domain isolated from human CFTRSemantic proximity Read ↗

Thermally unstable gating of the most common cystic fibrosis mutant channel (ΔF508): "rescue" by suppressor mutations in nucleotide binding domain 1 and by constitutive mutations in the cytosolic loops.Semantic proximity Read ↗

Selective Binding of HSC70 and its Co-Chaperones to Structural Hotspots on CFTRSemantic proximity Read ↗

Mechanism of CFTR correction by type I folding correctorsSemantic proximity Read ↗

Mechanism of CFTR correction by type I folding correctors.Semantic proximity Read ↗

Single-molecule dissection of CFTR folding defects and pharmacological rescue.Semantic proximity Read ↗

Conformational and temperature-sensitive stability defects of the delta F508 cystic fibrosis transmembrane conductance regulator in post-endoplasmic reticulum compartments.Semantic proximity Read ↗

Manipulating the folding pathway of delta F508 CFTR using chemical chaperones.Semantic proximity Read ↗

Single-molecule dissection of CFTR folding defects and pharmacological rescueSemantic proximity Read ↗

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channelSemantic proximity Read ↗

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