NHE-RF1 protein rescues F508-CFTR function
نویسندگان
چکیده
Florian Bossard,* Amal Robay,* Gilles Toumaniantz, Shehrazade Dahimene, Frédéric Becq, Jean Merot, and Chantal Gauthier Institut National de la Santé et de la Recherche Médicale Unité 533, l’ Institut du Thorax, Faculté de Médecine, Nantes; Centre National de la Recherche Scientifique Unité Mixte de Recherches 6187, Institut de Physiologie et Biologie Cellulaires, Université de Poitiers, Poitiers; and Faculté des Sciences et Techniques, Université de Nantes, Nantes, France
منابع مشابه
Mammalian osmolytes and S-nitrosoglutathione promote Delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) protein maturation and function.
In cystic fibrosis, the absence of functional CFTR results in thick mucous secretions in the lung and intestines, as well as pancreatic deficiency. Although expressed at high levels in the kidney, mutations in CFTR result in little or no apparent kidney dysfunction. In an effort to understand this phenomenon, we analyzed Delta F508 CFTR maturation and function in kidney cells under conditions t...
متن کاملc-Cbl reduces stability of rescued ∆F508-CFTR in human airway epithelial cells
CFTR is a PKA activated Cl(-) channel expressed in the apical membrane of fluid transporting epithelia. We previously demonstrated that c-Cbl decreases CFTR stability in the plasma membrane by facilitating its endocytosis and lysosomal degradation in human airway epithelium. The most common mutation associated with cystic fibrosis, deletion of Phe508 (∆F508), leads to a temperature sensitive bi...
متن کاملMechanisms for Rescue of Correctable Folding Defects in CFTR F508
Premature degradation of CFTR F508 causes cystic fibrosis (CF). CFTR F508 folding defects are conditional and folding correctors are being developed as CF therapeutics. How the cellular environment impacts CFTR F508 folding efficiency and the identity of CFTR F508’s correctable folding defects is unclear. We report that inactivation of the RMA1 or CHIP ubiquitin ligase permits a pool of CFTR F5...
متن کاملDelta F508 CFTR pool in the endoplasmic reticulum is increased by calnexin overexpression.
The most common cystic fibrosis transmembrane conductance regulator (CFTR) mutant in cystic fibrosis patients, Delta F508 CFTR, is retained in the endoplasmic reticulum (ER) and is consequently degraded by the ubiquitin-proteasome pathway known as ER-associated degradation (ERAD). Because the prolonged interaction of Delta F508 CFTR with calnexin, an ER chaperone, results in the ERAD of Delta F...
متن کاملInhibition of protein kinase CK2 closes the CFTR Cl channel, but has no effect on the cystic fibrosis mutant deltaF508-CFTR.
BACKGROUND Deletion of phenylalanine-508 (DeltaF508) from the first nucleotide-binding domain (NBD1) in the wild-type cystic fibrosis (CF) transmembrane-conductance regulator (wtCFTR) causes CF. However, the mechanistic relationship between DeltaF508-CFTR and the diversity of CF disease is unexplained. The surface location of F508 on NBD1 creates the potential for protein-protein interactions a...
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تاریخ انتشار 2007