Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Permeation through the CFTR chloride channel.

N A McCarty1

  • 1Department of Physiology, Emory University School of Medicine, Atlanta, GA 30322-3110, USA. NMCC@physio.emory.edu

The Journal of Experimental Biology
|June 14, 2000
PubMed
Summary

The cystic fibrosis transmembrane conductance regulator (CFTR) protein forms a Cl(-) channel. This review explores CFTR channel pore structure and ion permeation mechanisms, crucial for understanding cystic fibrosis and related diseases.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Bacterial Sphingomyelinase is a State-Dependent Inhibitor of the Cystic Fibrosis Transmembrane conductance Regulator (CFTR).

Scientific reports·2017
Same author

High-sweat Na+ in cystic fibrosis and healthy individuals does not diminish thirst during exercise in the heat.

American journal of physiology. Regulatory, integrative and comparative physiology·2011
Same author

Inhibition of ClC-2 chloride channels by a peptide component or components of scorpion venom.

The Journal of membrane biology·2006
Same author

Time-dependent interactions of glibenclamide with CFTR: kinetically complex block of macroscopic currents.

The Journal of membrane biology·2005
Same author

Steady-state interactions of glibenclamide with CFTR: evidence for multiple sites in the pore.

The Journal of membrane biology·2004
Same author

CFTR: covalent and noncovalent modification suggests a role for fixed charges in anion conduction.

The Journal of general physiology·2001

Area of Science:

  • Biophysics
  • Molecular Biology
  • Cell Biology

Background:

  • The cystic fibrosis transmembrane conductance regulator (CFTR) protein functions as a chloride channel in epithelial cells.
  • CFTR mutations cause cystic fibrosis, affecting ~30,000 in the US.
  • CFTR dysfunction is implicated in secretory diarrhea and polycystic kidney disease.

Purpose of the Study:

  • To review the current understanding of ion transport in wild-type CFTR channels.
  • To discuss experimental methods used to investigate the CFTR pore.
  • To present a proposed CFTR structure based on ion selectivity and blockade data.

Main Methods:

  • Literature review of existing research on CFTR function and structure.
  • Analysis of experimental approaches for studying ion permeation.
  • Integration of data on ion selectivity and pore blockade.

Main Results:

  • The precise structural elements forming the CFTR pore remain incompletely understood.
  • Specific amino acid residues involved in ion permeation are yet to be fully identified.
  • A proposed model integrates current knowledge on CFTR ion selectivity and pore blockade.

Conclusions:

  • Further research is needed to elucidate the detailed structure and function of the CFTR channel pore.
  • Understanding CFTR permeation mechanisms is vital for developing therapies for cystic fibrosis and related disorders.
  • The review synthesizes current data to propose a structural framework for CFTR ion transport.

Related Experiment Videos