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Related Experiment Video

Updated: Jan 29, 2026

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

CFTR structure, stability, function and regulation.

Xin Meng¹, Jack Clews¹, Anca D Ciuta¹

¹School of Biological Sciences, Faculty of Biology Medicine and Health, Michael Smith Building, The University of Manchester, Oxford Road, Manchester M13 9PL, UK.

Biological Chemistry

|February 10, 2019

Summary

This summary is machine-generated.

The F508del mutation impacts cystic fibrosis transmembrane conductance regulator (CFTR) protein stability, not its 3D structure. This suggests a new model for CFTR channel gating involving the protein's disordered regulatory region.

Keywords:

ABC transporter CFTR electron microscopy ion channel membrane protein structure

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Last Updated: Jan 29, 2026

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

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Area of Science:

Biochemistry
Structural Biology
Genetics

Background:

Cystic fibrosis transmembrane conductance regulator (CFTR) is an ATP-binding cassette protein functioning as an ion channel.
Mutations in CFTR cause cystic fibrosis, a prevalent genetic disorder, with F508del mutation affecting ~90% of patients.

Purpose of the Study:

To investigate the structural impact of the F508del mutation on CFTR.
To explore CFTR conformation and gating mechanisms.

Main Methods:

Analysis of cryo-electron microscopy studies on CFTR.
Investigation of CFTR structure under varying phosphorylation states and in the presence of NHERF1.

Main Results:

The F508del mutation primarily affects CFTR stability rather than its 3D folded state.
CFTR exhibits both outward-facing and inward-facing conformations under diverse experimental conditions.
Cryo-EM studies revealed conformational differences in CFTR despite similar experimental setups.

Conclusions:

The study favors a channel gating model where the disordered regulatory region of CFTR acts as a channel plug.
Findings provide insights into CFTR dysfunction in cystic fibrosis and potential therapeutic targets.