Controlling CFTR protein folding
نویسندگان
چکیده
منابع مشابه
Protein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions
Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...
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 کاملMechanisms of CFTR Folding at the Endoplasmic Reticulum
In the past decade much has been learned about how Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) folds and misfolds as the etiologic cause of cystic fibrosis (CF). CFTR folding is complex and hierarchical, takes place in multiple cellular compartments and physical environments, and involves several large networks of folding machineries. Insertion of transmembrane (TM) segments into...
متن کاملCorrectors promote folding of the CFTR in the endoplasmic reticulum.
Cystic fibrosis (CF) is most commonly caused by deletion of a residue (DeltaF508) in the CFTR (cystic fibrosis transmembrane conductance regulator) protein. The misfolded mutant protein is retained in the ER (endoplasmic reticulum) and is not trafficked to the cell surface (misprocessed mutant). Corrector molecules such as corr-2b or corr-4a are small molecules that increase the amount of funct...
متن کاملAnalysis of CFTR folding and degradation in transiently transfected cells.
Misfolding and premature degradation of F508del-CFTR is the major cause of cystic fibrosis. Components of the ubiquitin-proteasome system function on the surface of the endoplasmic reticulum to select misfolded proteins for degradation. The folding status of F508del-CFTR is monitored by at least two ER quality control checkpoints. The ER-associated Derlin-1/RMA1 E3 complex appears to recognize ...
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ژورنال
عنوان ژورنال: Genome Biology
سال: 2002
ISSN: 1465-6906
DOI: 10.1186/gb-spotlight-20020411-01