scholarly journals Modulation of Mature Cystic Fibrosis Transmembrane Regulator Protein by the PDZ Domain Protein CAL

2003 ◽  
Vol 279 (3) ◽  
pp. 1892-1898 ◽  
Author(s):  
Jie Cheng ◽  
Hua Wang ◽  
William B. Guggino
Keyword(s):  
Cystic Fibrosis ◽  
Pdz Domain ◽  
Cystic Fibrosis Transmembrane Regulator ◽  
Regulator Protein ◽  
Domain Protein ◽  
Cystic Fibrosis Transmembrane

Infrared biomarkers of impaired cystic fibrosis transmembrane regulator protein biogenesis

2019 ◽  
Vol 13 (1) ◽  
Author(s):  
Giuseppe Bellisola ◽  
Sara Caldrer ◽  
Mariangela Cestelli‐Guidi ◽  
Gianfelice Cinque
Keyword(s):  
Cystic Fibrosis ◽  
Cystic Fibrosis Transmembrane Regulator ◽  
Regulator Protein ◽  
Protein Biogenesis ◽  
Cystic Fibrosis Transmembrane

Cystic fibrosis

2020 ◽  
pp. 4151-4165
Author(s):  
Andrew Bush ◽  
Caroline Elston
Keyword(s):  
Cystic Fibrosis ◽  
Sodium Bicarbonate ◽  
European Population ◽  
Chloride Ions ◽  
Cystic Fibrosis Transmembrane Regulator ◽  
Chromosome 7 ◽  
Cystic Fibrosis Gene ◽  
Inherited Disease ◽  
Regulator Protein ◽  
Cystic Fibrosis Transmembrane

Cystic fibrosis (CF) is a recessively inherited disease caused by mutations in the cystic fibrosis gene, located on the long arm of chromosome 7, which codes for a membrane protein—the cystic fibrosis transmembrane regulator protein—that is a chloride channel. More than 2,000 CF mutations have been identified, with the Δ‎F508 mutation being the most common of around 200 mutations that definitely cause disease (70% of CF chromosomes in the European population). Birth incidence varies with country of origin from 1 in 2,000 to 1 in 100,000. The most popular hypothesis is that mutant cystic fibrosis transmembrane regulator protein fails to transport chloride ions normally, and there is secondary impairment of sodium, bicarbonate, and water transport.

Cystic fibrosis

2010 ◽  
pp. 3353-3364
Author(s):  
Andrew Bush ◽  
Caroline Elston
Keyword(s):  
Cystic Fibrosis ◽  
Membrane Protein ◽  
Chloride Channel ◽  
Cystic Fibrosis Transmembrane Regulator ◽  
Chromosome 7 ◽  
Cystic Fibrosis Gene ◽  
Inherited Disease ◽  
Regulator Protein ◽  
Cystic Fibrosis Transmembrane

Cystic Fibrosis (CF) is a recessively inherited disease caused by mutations in the cystic fibrosis gene, located on the long arm of chromosome 7, which codes for a membrane protein—the cystic fibrosis transmembrane regulator protein (CFTR)—that is a chloride channel. Around 1300 CF mutations have been identified, with the ...

scholarly journals Transcytosis maintains CFTR apical polarity in the face of constitutive and mutation-induced basolateral missorting

2018 ◽  
Author(s):  
Aurélien Bidaud-Meynard ◽  
Florian Bossard ◽  
Andrea Schnúr ◽  
Ryosuke Fukuda ◽  
Guido Veit ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Pdz Domain ◽  
Transmembrane Conductance Regulator ◽  
Transmembrane Conductance ◽  
Airway Epithelia ◽  
Apical Polarity ◽  
The Face ◽  
Domain Protein ◽  
Polarized Delivery ◽  
Cystic Fibrosis Transmembrane

SUMMARYApical polarity of cystic fibrosis transmembrane conductance regulator (CFTR) is essential for solute and water transport in secretory epithelia and can be impaired in human diseases. Maintenance of apical polarity in the face of CFTR non-polarized delivery and compromised apical retention of mutant CFTRs lacking PDZ-domain protein (NHERF1) interaction, remains enigmatic. Here we show that basolateral CFTR delivery originates from biosynthetic (~35%) and endocytic (~65%) recycling missorting. Basolateral channels are retrieved via basolateral-to-apical transcytosis, enhancing CFTR apical expression by two-fold and suppressing its degradation. CFTR transcytosis is microtubule-dependent but independent of Myo5B-, Rab11- and NHERF1 binding to its C-terminal DTRL motif in airway epithelia. Increased basolateral delivery due to compromised apical recycling and accelerated internalization upon impaired NHERF1-CFTR association is largely counterbalanced by CFTR efficient basolateral internalization and apical transcytosis. Thus, transcytosis represents a previously unrecognized but indispensable mechanism for maintaining CFTR apical polarity by attenuating its constitutive and mutation-induced basolateral missorting.

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