EurekaMag.com logo
+ Site Statistics
References:
53,869,633
Abstracts:
29,686,251
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on LinkedInFollow on LinkedIn

+ Translate

Identification of molecular determinants that modulate trafficking of DeltaF508 CFTR, the mutant ABC transporter associated with cystic fibrosis



Identification of molecular determinants that modulate trafficking of DeltaF508 CFTR, the mutant ABC transporter associated with cystic fibrosis



Cell Biochemistry and Biophysics 42(1): 41-53



Cystic fibrosis is a life-shortening inherited disorder associated primarily with a three-base in frame deletion that eliminates Phe508 in the ABC transporter, cystic fibrosis transmembrane conductance regulator (CFTR). Mutant CFTR, designated deltaF508 CFTR, is misprocessed and retained intracellularly. It is unclear what causes the trafficking impairment despite extensive investigative effort and the disease's prevalence.

(PDF emailed within 0-6 h: $19.90)

Accession: 012173400

Download citation: RISBibTeXText

PMID: 15673927

DOI: 10.1385/CBB:42:1:041



Related references

ERp29 regulates DeltaF508 and wild-type cystic fibrosis transmembrane conductance regulator (CFTR) trafficking to the plasma membrane in cystic fibrosis (CF) and non-CF epithelial cells. Journal of Biological Chemistry 286(24): 21239-21253, 2011

Inhibition of protein kinase CK2 closes the CFTR Cl channel, but has no effect on the cystic fibrosis mutant deltaF508-CFTR. Cellular Physiology and Biochemistry 24(5-6): 347-360, 2010

Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules. American Journal of Physiology. Lung Cellular and Molecular Physiology 290(6): L1117-L1130, 2006

A domain mimic increases DeltaF508 CFTR trafficking and restores cAMP-stimulated anion secretion in cystic fibrosis epithelia. American Journal of Physiology. Cell Physiology 287(1): C192-C199, 2004

Design and synthesis of a hybrid potentiator-corrector agonist of the cystic fibrosis mutant protein DeltaF508-CFTR. Bioorganic & Medicinal Chemistry Letters 20(1): 87-91, 2010

Mild processing defect of porcine DeltaF508-CFTR suggests that DeltaF508 pigs may not develop cystic fibrosis disease. Biochemical and Biophysical Research Communications 373(1): 113-118, 2008

Na+/H+ exchanger regulatory factor isoform 1 overexpression modulates cystic fibrosis transmembrane conductance regulator (CFTR) expression and activity in human airway 16HBE14o- cells and rescues DeltaF508 CFTR functional expression in cystic fibrosis cells. Journal of Biological Chemistry 280(49): 40925-40933, 2005

Functional activation of the cystic fibrosis trafficking mutant DF508-CFTR by overexpression. American Journal of Physiology 268: 15-L624, 1995

Correctors of the basic trafficking defect of the mutant F508del-CFTR that causes cystic fibrosis. Current Opinion in Chemical Biology 17(3): 353-360, 2014

Morphological changes in the vas deferens and expression of the cystic fibrosis transmembrane conductance regulator (CFTR) in control, deltaF508 and knock-out CFTR mice during postnatal life. Molecular Reproduction and Development 55(2): 125-135, 2000

Functional activation of the cystic fibrosis trafficking mutant delta F508-CFTR by overexpression. American Journal of Physiology 268(4 Pt 1): L615-L624, 1995

Global proteomic approach unmasks involvement of keratins 8 and 18 in the delivery of cystic fibrosis transmembrane conductance regulator (CFTR)/deltaF508-CFTR to the plasma membrane. Proteomics 4(12): 3833-3844, 2004

Low temperature and chemical rescue affect molecular proximity of DeltaF508-cystic fibrosis transmembrane conductance regulator (CFTR) and epithelial sodium channel (ENaC). Journal of Biological Chemistry 287(20): 16781-16790, 2012

Physiology of a cystic fibrosis DELTAF508-CFTR mouse model. Greger, R [Author], Jentsch, T J [Author] Nova Acta Leopoldina; Ion channels and disease : 145-146, 1997